Sample Test

BIOCHEMISTRY TEST
You have 546 questions in this exam.

1. Increasing the concentration of dGTP directly causes rionucleotide reductase to
!. increase the rate of "roduction of dG#P.
$. increase the rate of "roduction of d!#P.
%. decrease the rate of "roduction of r%#P.
#. decrease the rate of "roduction of d!#P.
&. increase the rate of "roduction of dTTP.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) ,as no direct effect -Increased dGTP increases d!TP "roduction. (hich eventually (ould
decrease /0/ activity overall. ut dGTP has no immediate effect on the en1yme exce"t to increase d!#P
formation2
*eedac+ %) ,as no direct effect -Increased dGTP increases d!TP "roduction. (hich eventually (ould
formation2
*eedac+ #) This rate increases
*eedac+ &) ,as no direct effect -Increased dGTP increases d!TP "roduction. (hich eventually (ould
formation2
3. Glycogen "hos"horylase is activated most directly y
!. e"ine"hrine.
$. "hos"horylase +inase.
%. "hos"horylase "hos"hatase.
#. c!4P.
&. glucagon.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) 'ee $
*eedac+ $) glucagon or e"ine"hrine 5556 increased c!4P 5556 active P7! 5556 active "hos"horylase
+inase 5556 active glycogen "hos"orylase
*eedac+ %) 'ee $
*eedac+ #) 'ee $
*eedac+ &) 'ee $
8. 9hich of the follo(ing cofactors is most directly concerned (ith a %:3 fixation reaction;
!. iotin
$. vitamin #
%. coen1yme !
#. thiamine "yro"hos"hate
&. li"oic acid
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) $iotin is a carrier of activated %:3 and is a com"onent of acetyl caroxylase. "ro"ionyl %o!
caroxylase. and "yruvate caroxylase.
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4. 9hich statement aout reactions cataly1ed y transaminases -aminotransferases2 is false;
!. The equilirium constant is close to 1.
$. The reaction involves a 'chiff ase intermediate.
%. Pyridoxal "hos"hate is covalently ound to the en1yme "rotein through the e"silon amino grou" of a
lysine residue.
#. The reactions are im"ortant for the iosynthesis of non5essential amino acids.
&. !mmonia is lierated.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) !minotransferases can "artici"ate in degradation or iosynthesis de"ending on sustrate
concentrations.
*eedac+ $)
*eedac+ %)
*eedac+ #) !minotransferases most commonly transfer amino grou"s to al"ha5+etoglutarate forming
glutamate. Glutamate can then e the amino grou" donor for amino acid iosynthesis.
*eedac+ &) *alse. an amino grou" is transferred to an al"ha5+eto acid.
5. The en1yme in muscle (hich is most directly stimulated y e"ine"hrine is
!. glycogen synthase.
$. "hos"hofructo+inase.
%. isocitrate dehydrogenase
#. glucose565"hos"hatase.
&. adenylate cyclase.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) inactivated due to e"ine"hrine.
*eedac+ $) decreased stimulation of P*751
*eedac+ %) very indirect modification
*eedac+ #) %hanges in its activity are determined y synthesis and degradation.
*eedac+ &) increased intracellular c!4P.
6. !cetyl5%o! regulates gluconeogenesis y activation of
!. "hos"hoenol"yruvate caroxy+inase.
$. "yruvate +inase.
%. "yruvate caroxylase.
#. lactate dehydrogenase.
&. fructose 1.65is"hos"hatase.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) 9hich cataly1es) "yruvate < %:3 5556 oxaloacetate.
*eedac+ #)
*eedac+ &)
=. 9hich com"ound does 0:T cross the inner mitochondrial memrane due to lac+ of a s"ecific trans"ort
"rotein;
!. malate
$. glutamine
%. 0!#,
#. citrate
&. !TP
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) 0!#, reducing "otential must e shuttled across the memrane y another molecule.
*eedac+ #)
*eedac+ &)
>. !ll of the follo(ing statements are correct (ith regard to chromatin &?%&PT
!. %ore nucleosomes consist of > histone "rotein molecules and aout 146 ase "airs of #0!.
$. ,istones have een highly conserved during evolution.
%. !lmost all of the #0! in a eu+aryotic cell is assemled into nucleosomes.
#. !ssemly of #0! into nucleosomes com"acts it aout 1@@5fold in length.
&. 0ucleosome cores are se"arated y variale amounts of lin+er #0!.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) see #
*eedac+ $) see #
*eedac+ %) see #
*eedac+ #) 0ucleosomes effect aout a 55= fold com"action of the length of the #0!
*eedac+ &) see #
A. 9hich is B&!'T li+ely to e characteristic of a regulated en1yme in a metaolic "ath(ay;
!. %ataly1es the slo(est ste" of the "ath(ay
$. ,as a short half5life in vivo
%. %oncentration is hormonally regulated
#. !ctivity under allosteric control
&. %ataly1es a "hysiologically reversile reaction
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &) Irreversile reactions are usually regulated. es"ecially those that involve !TP.
1@. 9hich of the follo(ing are exam"les of tertiary -8C2 structure; 1. the sequence of amino acids in a
"rotein 3. the al"ha5helix of hemogloin 8. the folding of al"ha5helix onto eta5sheet of triose "hos"hate
isomerase 4. hydrogen onding of one eta 5sheet to another eta5sheet 5. Duxta"osition of amino acids
that are se"arated y a Elong distanceE in "rimary -1C2 structure 6. the un5ordered "ortions of caroxy
"e"tidase ! =. Duxta"osition of hemogloin eta5= Glu (ith al"ha56> !sn
!. all the even5numered items
$. all the odd5numered items
%. 8. 4. and 5
#. 8. 4. 5. and =
&. 8. 4. 5. 6. and =
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) 15"rimary. 35secondary. 65hard to classify55"rimary or secondary. =5quaternary
*eedac+ #)
*eedac+ &)
11. The ,1 histone
!. is one of the four histones in the nucleosome core.
$. hel"s form the octamer nucleosome com"lex.
%. is rich in acidic amino acid residues.
#. is "resent at a 1)1 (eight ratio (ith #0!.
&. hel"s fold or staili1e the Eeads5on5a5stringE structure into higher order structures.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) 0o. the core histones are ,3!. ,3$. ,8. and ,4
*eedac+ $) 0o. the octamer contains only ,3!. ,3$. ,8. and ,4
*eedac+ %) It is rich in asic amino acids
*eedac+ #) :verall. all histones -,1 and ,3!. ,3$. ,8. and ,42 are aout 1)1 (ith #0!
*eedac+ &)
13. 9hich mitochondrial en1yme requires acetyl5%o! as a sustrate;
!. %itrate synthase
$. 'uccinyl5%o! synthase
%. 'uccinic dehydrogenase
#. Pyruvate dehydrogenase
&. Isocitrate dehydrogenase
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) %ataly1es) acetyl %o! < oxaloacetate 5556 citrate.
*eedac+ $) %o! is required coen1yme. ut not acetyl %o!.
*eedac+ %)
*eedac+ #) Produces acetyl %o! from "yruvate.
*eedac+ &)
18. Transfer of the methyl grou" from 55methyl tetrahydrofolate to homocysteine to form methionine
requires
!. 0!#P,
$. vitamin $13
%. *!#
#. "yridoxal "hos"hate
&. none of the aove
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $) 4ethycoalamin. a derivative of $13. is the coen1yme that mediates the transfer of methyl
grou"s in methionine iosynthesis.
*eedac+ %)
*eedac+ #) !minotransferases require this coen1yme.
*eedac+ &)
14. !ll of the follo(ing are true of acterial "lasmids or e"isomes &?%&PT
!. &"isomes li+e the * factor can e transferred from one cell to another.
$. Plasmids or e"isomes can confer resistance to many antiiotics simultaneously.
%. Plasmids or e"isomes can e transferred from one s"ecies of acteria to another.
#. 'ince "lasmids must e re"licated. they confer a disadvantage to their hosts and can therefore e
ex"ected to disa""ear from human "athogens soon.
&. Genes can e transferred from acterial genomes to "lasmids at a lo( frequency.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) This is true. they can "ass through a "ilus into another cell.
*eedac+ $) This is true.
*eedac+ %) This is true
*eedac+ #) The disadvantages caused y FcarryingG "lasmids are out(eighed y the advantages they
"rovideH this advantage increases as (e use antiiotics.
*eedac+ &) 'trange ut true.
15. If one mole of glucose is metaoli1ed to caron dioxide and (ater via glycolysis and the tricaroxylic
acid cycle. and the glycerol "hos"hate shuttle is o"erative. the net conversion of !#P -or equivalent2 to
!TP -or equivalent2 (ould theoretically e
!. 13 moles.
$. 34 moles.
%. 83 moles.
#. 86 moles.
&. 8> moles.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #) The 30!#, "roduced y glycolysis are converted to 3*!#,3 in the mitochondria y the
glycerol "hos"hate shuttle. so they are (orth 3!TP each.
*eedac+ &) 9ith the malate5as"artate shuttle the 30!#, from glycolysis are converted to 30!#, in the
mitochondria. and are (orth 8!TP each.
16. The cofactor for transamination is
!. nicotinamide.
$. iotin.
%. thiamine "yro"hos"hate.
#. "yridoxal "hos"hate.
&. vitamin $13.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #) ! vitamin $6 derrivative that is a "rosthetic grou" for each transaminase.
*eedac+ &)
1=. 9hich en1yme cataly1es a reaction in (hich caron dioxide -or icaronate2 is neither a sustrate nor
a "roduct;
!. isocitrate dehydrogenase
$. "yruvate caroxylase
%. caroxy"e"tidase
#. "hos"hoenol"yruvate caroxy+inase
&. al"ha5+etoglutarate dehydrogenase
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) %:3 "roduced.
*eedac+ $) %:3 is a sustrate.
*eedac+ %) %leaves "e"tide onds. no %:3 involved.
*eedac+ #) %:3 "roduced.
*eedac+ &) %:3 "roduced.
1>. 55"hos"horiosyl515"yro"hos"hate -P/PP2 is an intermediate in
!. the de novo synthesis of "urine nucleotides.
$. the de novo synthesis of "yrimidine nucleotides.
%. the salvage "ath(ay for the synthesis of "urine nucleotides.
#. ! and %.
&. !. $ and %.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) True -it is activated as the committed ste" for "urine synthesis2. ut so are $ and %
*eedac+ $) True -orotidylate is formed y reacting the free ase (ith P/PP2. ut so are ! and %
*eedac+ %) True -P/PP reacts (ith free ases li+e guanine and hy"oxanthine through ,GP/Tase2. ut so
are ! and $.
*eedac+ #) True. ut $ is also correct
*eedac+ &)
1A. 9hich statements are *!B'&; In mitochondria. tricaroxylic acid cycle reactions generally "roceed
more
-12 ra"idly as the !#P concentration rises.
-32 slo(ly as the !#P concentration rises.
-82 slo(ly as the 0!#, concentration rises.
-42 ra"idly as the 0!#, concentration rises.
-52 ra"idly as the oxaloacetate concentration increases.
!. 1 and 8
$. 3 and 4
%. 8 and 5
#. 1 and 4
&. 3 and 5
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $) ,igh levels of !TP and 0!#, signal that the cellIs energy level is high. high !#P and 0!#<
signal that more energy is needed.
*eedac+ %)
*eedac+ #)
*eedac+ &)
3@. In Besch50yhan syndrome. lac+ of ,GP/Tase activity should result in higher than normal tissue
concentrations of all of the follo(ing &?%&PT
!. adenine.
$. guanine.
%. uric acid.
#. hy"oxanthine.
&. P/PP.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) !denine levels are not directly affected y loss of this en1yme.
*eedac+ $) This sustrate for ,GP/Tase (ould accumulate anormally in the asence of the en1yme.
*eedac+ %) Increased hy"oxanthine leads to increased xanthine and therefore increased uric acid.
*eedac+ #) This sustrate for ,GP/Tase (ould accumulate anormally in the asence of the en1yme.
*eedac+ &) This sustrate for ,GP/Tase (ould accumulate anormally in the asence of the en1yme.
31. 9hich of the follo(ing re"resents the correct numer of moles of "roducts formed as one mole of
acetate -in the form of acetyl5%o!2 moves through one turn of the citric acid cycle; -res"ectively2
GTP
%:3
0!#,
*!#,3
!. 1 1 8 1
$. 3 3 8 1
%. 1 3 8 1
#. 1 3 3 1
&. 1 1 3 3
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) 4emori1e the cycle.
*eedac+ #)
*eedac+ &)
33. ,o( many net moles of !TP are "roduced "er glucose equivalent (hen glycogen is the sustrate for
anaeroic glycolysis;
!. @
$. 1
%. 3
#. 8
&. 53
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #) glycogen 5556 glucose515"hos"hate 5556 glucose565"hos"hate 5556 glycolysis. $ecause
glycose565"hos"hate enters glycolysis the reaction cataly1ed y gluco+inase or hexo+inase is not carried
out and one less !TP is used.
*eedac+ &)
38. :ne of the strands of a doule5stranded. 1@ +" #0! du"lex has the follo(ing numers of ase
residues) adenine-a2 5 8>@@. thymine-t2 5 36@@. The ase com"osition of the (hole doule5stranded
molecule (ill e
!. a 5 53@@. t 5 53@@. g 5 4>@@. c 5 4>@@
$. a 5 =6@@. t 5 =6@@. g 5 34@@. c 5 34@@
%. a 5 64@@. t 5 64@@. g 5 86@@. c 5 86@@
#. a 5 64@@. t 5 86@@. g 5 64@@. c 5 86@@
&. There is not enough information to determine the overall ase com"osition
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) If one strand has 8>@@ ! and 36@@ T. the other strand has 8>@@ T and 36@@ !. so the du"lex
has 64@@ ! and 64@@ T. (ith the remainder eing G and % -86@@ each2.
*eedac+ $) If one strand has 8>@@ ! and 36@@ T. the other strand has 8>@@ T and 36@@ !. so the du"lex
*eedac+ %)
*eedac+ #) If one strand has 8>@@ ! and 36@@ T. the other strand has 8>@@ T and 36@@ !. so the du"lex
*eedac+ &) If one strand has 8>@@ ! and 36@@ T. the other strand has 8>@@ T and 36@@ !. so the du"lex
34. ! maDor control "oint of the citric acid cycle is exerted at the level of
!. succinate dehydrogenase.
$. citrate synthase.
%. succinyl %o! synthase.
#. malate dehydrogenase.
&. aconitase.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $) %itrate synthase. isocitrate dehydrogenase. and al"ha5+etoglutarate dehydrogenase are the
regulated en1ymes of T%! cycle.
*eedac+ %)
*eedac+ #)
*eedac+ &)
35. 'econdary structure of "roteins
!. is maintained y hydrogen onds.
$. refers to "roteins consisting of t(o -or more2 suunits held together y noncovalent forces.
%. encom"asses any hydrogen5onded interaction found in "roteins.
#. refers to "roteins consisting of one or more "oly"e"tide chains "lus a non"rotein moiety.
&. is found only in firous "roteins.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) al"ha5helix and eta5sheet.
*eedac+ $) This is quaternary.
*eedac+ %) 0o. ,5ond interactions et(een residues far a"art linearly (ould e tertiary interactions.
*eedac+ #) This is quaternary.
*eedac+ &) !ny "rotein.
36. &ach of the follo(ing statements concerning #0! is true &?%&PT (hich one;
!. % does not have to equal G in single stranded #0!.
$. #0! can e found in either circular or linear forms.
%. The t(o #0! strands of the doule helix are anti"arallel.
#. ,ydrogen onds alone hold the #0! helix together.
&. $ase "airs lie in a "lane "er"endicular to the long axis of the helix.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) This is true. *or exam"le. a single5stranded #0! could e all % and have no G.
*eedac+ $) This is trueH most acterial "lasmids are circles (hile most mammalian chromosomes are
linear.
*eedac+ %) Please donIt tell me you "ic+ed this one. I Dust donIt (ant to +no(.
*eedac+ #) 0o. they contriute ut they are only one "art of the "icture.
*eedac+ &) This is true.
3=. The reduction "otential for a reaction
!. is an oxidation "otential.
$. is unrelated to the free energy of the reaction.
%. is negative for a s"ontaneous "rocess.
#. can e used to decide if one sustance (ill reduce another.
&. is not de"endent on reactant andJor "roduct concentration.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) ,as the o""osite sign of the reduction "otential.
*eedac+ $)
*eedac+ %) Positive for a s"ontaneous redox reaction.
*eedac+ #) 4ore negative -smaller2 reduction "otentials donate electrons to more "ositive -larger2
reduction "otentials.
*eedac+ &)
3>. Glutamine
!. is not incor"orated into "roteins ecause there is no codon or t/0! for glutamine.
$. is the "rinci"al donor of amino grou"s in transamination reactions.
%. donates its al"ha5amino grou" in the de novo iosynthesis of oth "urine and "yrimidine nucleotides.
#. is synthesi1ed from glutamate "rimarily in the liver.
&. re"resents an im"ortant non5toxic trans"ort form of ammonia.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) There are codons and t/0!Is for oth glutamine and glutamate.
*eedac+ $) Glutamine is the ultimate "roduct of tissue transamination. Glutamine is trans"orted to the
liver (here nitrogen metaolism to urea ta+es "lace.
*eedac+ %) #onates its gamma5amide in oth syntheses.
*eedac+ #) 'ynthesis occurs "rimarily in the tissues and then glutamine is ro+en do(n into glutamate
and ammonia in the liver.
*eedac+ &) 'ee $.
3A. !s a cell initiates #0! re"lication. it contains sufficient "ools of d0TPs to com"lete
!. aout 1K or less of #0! re"lication (ithout ma+ing ne( d0TPs.
$. aout 1@K of #0! re"lication (ithout ma+ing ne( d0TPs.
%. 1@@K of #0! re"lication (ithout ma+ing ne( d0TPs.
#. aout 1@ times more d0TPs than it needs to re"licate the genome once.
&. no re"lication at all.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) !out @.1K in mammals. 1K in acteria
*eedac+ $) !out @.1K in mammals. 1K in acteria
*eedac+ %) !out @.1K in mammals. 1K in acteria
*eedac+ #) !out @.1K in mammals. 1K in acteria
*eedac+ &) !out @.1K in mammals. 1K in acteria
8@. The uncou"ling of oxidative "hos"horylation in the human might e of "hysiological im"ortance
ecause it
!. allo(s storage of nutrients.
$. "roduces (ater.
%. increases caron dioxide level in the lood.
#. "roduces heat.
&. raises the oxygen level in the lood.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #) The energy "roduced y electron trans"ort is released as heat rather than eing used to
synthesi1e !TP.
*eedac+ &)
81. The condition of B!%T:'& I0T:B&/!0%& can e caused y defective or deficient
!. lactose
$. L#P5galactose e"imerase
%. galactose515"hos"hate uridyl transferase
#. lactase
&. galactase
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
83. #uring the second day of a fast. after liver glycogen is de"leted. lood glucose
!. is derived mainly from fatty acids of adi"ose tissue.
$. is derived mainly from muscle glycogen.
%. is derived mainly from the amino acids of liver "roteins.
#. falls to lo( levels -e.g.. 3@ mgJ1@@ ml2 until eating is resumed.
&. is derived mainly from the amino acids of muscle "roteins.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) !fter a""roximately 8 (ee+s of starvation muscle almost exclusively oxidi1es fatty acids for
energy.
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &) /a"id rea+do(n of muslce "rotein ta+es "lace the first fe( days of starvation to "rovide
amino acids for gluconeogenesis.
88. ! com"lete lac+ of adenosine deaminase causes '%I#) severe comined immuno5deficiency. 9hich of
the follo(ing is B&!'T true;
!. Boss of the en1yme causes increased levels of d!TP ecause there is less turnover of adenosine
nucleosides in general.
$. Increased d!TP decreases the concentration of all r0TPs. loc+ing /0! synthesis.
%. Increased d!TP inhiits rionucleotide reductase. such that de novo "roduction of all d0#Ps is inhiited.
#. !denosine deaminase loss causes '%I# ecause T cells are "articularly sensitive to #0! re"lication
inhiition.
&. It is not clear (hy adenosine deaminase loss affects T cells so s"ecifically since other cells have the
same +ind of nucleotide synthesis regulation and might e ex"ected to e equally affected.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) This is true. failure to degrade adenosine forms causes their concentrations to rise.
*eedac+ $) Bac+ of d0TPs loc+s #0! synthesis. not /0! synthesis
*eedac+ %) This is true. d!TP levels rise -see !2 (hich shuts do(n all /0/ activities
*eedac+ #) This is trueH the reason is not fully +no(n ut it is oserved to e the case.
*eedac+ &) This is true. see #.
84. In the oxidation of 0!#, y the electron trans"ort system. energy released is cou"led to the
formation of !TP from !#P "lus inorganic "hos"hate. *or every mole of 0!#, oxidi1ed. ho( many moles
of !TP formed are formed;
!. 1
$. 5
%. 8
#. 6
&. 0one of the aove
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) This is for 0!#, in the mitochondria. 0!#, outside of the mitochondria "roduce different
numers of !TP de"ending on the shuttle system used to transfer the reducing "otential from the cytosol
to the mitochondria.
*eedac+ #)
*eedac+ &)
85. In analysis of isoen1ymes of serum %P7 for diagnosis of an !4I
!. %P7 aove six times normal total %P7 indicates an !4I.
$. %P7544 aove four times normal total %P7 indicates an !4I.
%. %P75$$ aove 1K of total normal. and total %P7 of six times normal %P7 indicates an !4I.
#. %P754$ aove 8K of total normal %P7 indicates an !4I.
&. Total %P7 aove six times normal. (ith %P7 $$ in the normal range indicates an !4I.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #) %P754$ is only 158K in other muscle. ut 1553@K in heart muscle.
*eedac+ &)
86. 9hich of the follo(ing is true aout the structure and "ro"erties of !TP;
!. The structure contains 8 "hos"hoanhydride onds and one glycosidic ond.
$. !t "hysiological ",. the molecule has a net charge of a""roximately 56.
%. The transfer of a "hos"horyl grou" -"hos"hate residue2 is the only iological reaction of !TP that
cleaves a high5energy ond.
#. The high free energy of hydrolysis results. in "art. from electrical re"ulsion et(een "hos"hate
residues.
&. The standard free energy of hydrolysis of !TP is highter than that of other all "hos"hate derivatives in
the glycolytic "ath(ay.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) 3 "hos"hoanhydride onds and one glycosidic ond.
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &) 0o. hydrolysis of P&P gives more energy than hydrolysis of !TP.
8=. 9hich of the follo(ing s"ecies of denatured #0! (ill renature most ra"idly in solution. under
a""ro"riate conditions of ionic strength. ",. and tem"erature;
!. ,uman liver nuclear #0!
$. Maccinia -viral2 #0!
%. &. coli #0!
#. Yeast nuclear #0!
&. 4ouse neuronal #0!
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) The /!T& of reannealing de"ends on the concentration of com"lementary strands. Given the
same overall #0! concentration -a fact that should have een stressed in this question2. the more
com"lex the genome the B:9&/ the concentration of any given sequence -and its com"lement2 so the
slo(er the renaturation. Therefore. the least com"lex genome (ill anneal the fastest. in this case the viral
#0! -$2.
*eedac+ $) The /!T& of reannealing de"ends on the concentration of com"lementary strands. Given the
#0! -$2.
*eedac+ %) The /!T& of reannealing de"ends on the concentration of com"lementary strands. Given the
#0! -$2.
*eedac+ #) The /!T& of reannealing de"ends on the concentration of com"lementary strands. Given the
#0! -$2.
*eedac+ &) The /!T& of reannealing de"ends on the concentration of com"lementary strands. Given the
#0! -$2.
8>. 9hen oxidative "hos"horylation in mitochondria is uncou"led
!. !4P is formed and :3 consum"tion sto"s.
$. the oxidation of acetyl %o! in the tricaroxylic acid cycle sto"s.
%. mitochondrial metaolism sto"s.
#. !TP synthesis sto"s ut :3 consum"tion continues.
&. the cytochromes lose their heme grou"s into the cyto"lasm.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #) &lectron trans"ort continues to reduce :3. ut the "roton gradient is not maintained so !TP
is not synthesi1ed.
*eedac+ &)
8A. :xaloacetate moves through the mitochondrial memrane
!. after conversion to glycerol "hos"hate.
$. y "assive diffusion.
%. after reaction (ith carnitine.
#. after oxidation to "yruvate.
&. after reduction to malate.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) #,!P < 0!#, 5556 glycerol585"hos"hate < 0!# in the glycerol"hos"hate shuttle.
*eedac+ $)
*eedac+ %) Bong5chain fatty acids are trans"orted into the mitochondria for oxidation y carnitine.
*eedac+ #)
*eedac+ &) The 4alate5!s"artate shuttle for 0!#,.
4@. The asence of (hich en1yme results in P7L -"henyl+etonuria2;
!. Tyrosine hydroxylase
$. !mino acid oxidase
%. Phenylalanine hydroxylase
#. Tyrosine transaminase
&. Phenylalanine transaminase
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) Phenylalanine is not hydroxylated to tyrosine. and uilds u" to toxic levels.
*eedac+ #)
*eedac+ &)
41. !ll of the follo(ing statements are consistent (ith the chemiosmotic hy"othesis of oxidative
"hos"horylation &?%&PT (hich one;
!. !gents (hich uncou"le oxidative "hos"horylation from electron trans"ort disru"t "ermeaility arriers
such that mitochondrial memranes ecome "ermeale to "rotons.
$. The term electrochemical gradient or "roton gradient o"erationally descries the free energy generated
y electron trans"ort (hich drives "hos"horylation of !#P.
%. Protons are transferred into the mitochondria during electron trans"ort estalishing a ", gradient.
#. Intact mitochondrial memranes are necessary for oxidative "hos"horylation to occur.
&. &lectron carriers of the electron trans"ort chain are vectorially oriented.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) Protons are transferred from the matrix to the intermemrane s"ace of the mitochondria.
*eedac+ #) The "roton gradient must e set u" across the inner memrane.
*eedac+ &)
43. 9hich statement aout the "yruvate dehydrogenase com"lex is true;
!. Bi"oamide functions in the decaroxylation of "yruvate.
$. %oen1yme ! is covalently ound to a lysine residue in one of the "roteins of the com"lex.
%. Phos"horylation cataly1ed y a +inase results in decreased activity.
#. 0!#, is an allosteric activator of "yruvate oxidation.
&. The function of *!# is to oxidi1e 0!#,.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) TPP functions in decaroxylationH li"oamide transfers the acetyl grou" to %o!.
*eedac+ $) Bi"oamide is ound to lysine.
*eedac+ %) Increased acetyl %o!J%o! or 0!#,J0!# ratios activate the +inase (hich "hos"horylates and
deactivates P#,.
*eedac+ #) Increased 0!#, causes indirect inhiition of P#,.
*eedac+ &) *!#,3 reduces 0!# to 0!#,.
48. 9hich of the follo(ing is the single most im"ortant factor accounting for the high rates of en1yme
catalysis;
!. &n1ymes ring the sustrate N'O into close "roximity of the coen1yme.
$. %ertain en1yme amino acid side chains interact (ith the sustrate and staili1ing reactive
intermediate-s2.
%. The Efree energyE of activation is increased during en1yme catalysis.
#. &n1ymes contain "rosthetic grou"s (hich "romote catalysis.
&. &n1ymes are gloular "roteins (hich contain hydro"hoic and hydro"hilic amino acids.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $) &n1ymes stalai1e the transition state.
*eedac+ %) !citvation energy is lo(ered y en1ymes.
*eedac+ #) True. ut not the est ex"lanation.
*eedac+ &) #oes not ex"lain catalysis.
44. :xidative "hos"horylation in mitochondria is carried out y en1ymes
!. on the outer memrane.
$. on the inner memrane.
%. in the matrix.
#. in the intermemrane s"ace.
&. all of the aove are correct..
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
45. 9hat change from normal is li+ely to result from the ingestion of ethanol;
!. increased reduction of "yruvate
$. increased conversion of eta5hydroxyutyrate to acetoacetate
%. decreased +etogenesis due to lac+ of acetyl5%o!
#. increased "roduction of oxaloacetate from malate
&. increased "roduction of dihydroxyacetone "hos"hate from glycerol "hos"hate
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) &thanol metaolism requires reduction of 0!# to 0!#, . and as in anaeroic glycolysis. 0!#
is regenerated y reduction of "yruvate to lactate.
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
46. Glucagon
!. is released from the "ancreas in res"onse to lo(ered lood glucose.
$. inactivates liver "hos"horylase.
%. increases glucose release from muscle glycogen.
#. utili1es c!4P as a second messenger in muscle cells.
&. increases glucose u"ta+e into he"atocytes.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $) !ctivates the "hos"horylase for glycogen degradation.
*eedac+ %) Glucagon does not affect muscle.
*eedac+ #) 'ee %.
*eedac+ &) Insulin increased glucose u"ta+e (hen lood glucose is high.
4=. 4uscle can carry out all of the follo(ing "rocesses &?%&PT
!. transamination of ranched chain amino acids.
$. synthesis of glycogen.
%. synthesis of glucose from alanine.
#. oxidation of +etone odies.
&. "hos"horylation of creatine.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) 4uscle cannot carry out gluconeogenesis ecause "yruvate caoxylase is found only in liver
and +idney cells.
*eedac+ #)
*eedac+ &)
4>. !ll of the follo(ing are li+ely to occur follo(ing the ingestion of a very large amount of carohydrate
&?%&PT
!. the synthesis of triacylglycerol in the liver.
$. the synthesis of glycogen in the liver.
%. the oxidation of glucose y the "entose "hos"hate "ath(ay in liver.
#. li"olysis in adi"ose tissue.
&. the synthesis and release of MB#B from the liver.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #) ,igh glucose levels lead to high insulin (hich su""orts synthesis of storage molecules. not
rea+do(n.
*eedac+ &)
4A. %atalysis y chymotry"sin de"ends on the concerted "artici"ation of three amino acid side chains
-catalytic triad2 (hich are contriuted y (hich of the follo(ing amino acids;
!. !rginine. histidine. and serine
$. ,istidine. serine. and glutamate
%. 'erine. glutamate. and as"artate
#. !s"artate. serine. and histidine
&. 'erine. histidine. and arginine
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #) 4emori1e it. 7no( the "art each "lays in the mechanism.
*eedac+ &)
5@. 9hich of the follo(ing is the most accurate descri"tion of "hos"hofructo+inase51;
!. This en1yme uses fructose565"hos"hate as a sustrate and converts it to fructose53.65 di"hos"hate.
$. This en1yme is inhiited y !TP. citrate. and fructose53.65i"hos"hate.
%. This en1yme cataly1es a fully reversile reaction under "hysiological conditions.
#. This activity of this en1yme is indirectly increased y cyclic !4P.
&. 0o statement aove is accurate.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) P*753 ma+es fructose53.65is"hos"hate. P*751 "roduces fructose51.65is"hos"hate.
*eedac+ $) Inhiited y !TP and citrate. stimulated y fructose53.65is"hos"hate and !4P.
*eedac+ %) The committed ste" of glycolysis. irreversile.
*eedac+ #) Indirectly decreased ecause increased c!4P causes P*753J*$P53 com"lex to act as a
"hos"hatase.
*eedac+ &)
51. !ll of the follo(ing amino acids are required as "recursors for collagen -"rocollagen2 synthesis &?%&PT
!. lysine.
$. glycine.
%. "roline.
#. hydroxy"roline.
&. "henylalanine.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) %ommonly hydroxylated to hydroxylysine in collagen.
*eedac+ $) *ound every third residue.
*eedac+ %) %ommonly hydroxylated to hydroxy"roline.
*eedac+ #) Proline is the "recursor (hich undergoes "osttranslational modification to hydroxy"roline.
*eedac+ &)
53. 9hich of the follo(ing statements is an accurate com"arison et(een chymotry"sinogen and
chymotry"sin;
!. %hymotry"sinogen has a single amino terminus and is inactive.
$. %hymotry"sinogen is a storage form of chymotry"sin and is active.
%. %hymotrysinogen and chymotry"sin are readily interconvertale forms of this hydrolase.
#. 4ore than one of the aove is an accurate statement.
&. 0one of the aove is an accurate statement.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) %hymotry"sinogen is a single "oly"e"tide chain that is cleaved to give chymotry"sin -8
chains that are lin+ed y 3 disulfide onds2.
*eedac+ $) %hymotry"sinogen is inactive.
*eedac+ %) 0o. cleavage of chymotry"sinogen to chymotry"sin is irreversile.
*eedac+ #)
*eedac+ &)
58. /eactions occurring during anaeroic GBY%:BY'I' in liver (hich require the in"ut -use of2 of !TP
include
!. "yruvate +inase and gluco+inase
$. "yruvate +inase and "hos"hofructo+inase
%. glyceraldehyde585"hos"hate dehydrogenase and "yruvate +inase
#. gluco+inase and "hos"hofructo+inase
&. gluco+inase and glyceraldehyde585"hos"hodehydrogenase
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) 'ee %.
*eedac+ $) 'ee %.
*eedac+ %) Glyceraldehyde585"hos"hate dehydrogenase "roduces 0!#,. "yruvate +inase "roduces !TP.
*eedac+ #)
*eedac+ &) 'ee %.
54. The conversion of the t(o nitrogen atoms of glutamine to the t(o nitrogen atoms of urea requires the
"artici"ation of urea cycle en1ymes and
!. glutaminase only.
$. glutamate dehydrogenase only.
%. glutaminase and as"artate aminotransferase -transaminase2.
#. glutaminase and glutamate dehydrogenase.
&. glutamate dehydrogenase and as"artate aminotransferase.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) :ne urea nitrogen comes from glutamine and enters the urea cycle as caramoyl "hos"hate.
the second nitrogen enters the cycle as as"artate.
*eedac+ #)
*eedac+ &)
55. 9hich molecule can donate a one5caron unit most directly to tetrahydrofolate;
!. serine
$. methionine
%. glutamate
#. histidine
&. choline
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
56. EInduced fitE is oserved during catalysis y
!. adenylate cyclase.
$. glycogen "hos"horylase EE.
%. chymotry"sin.
#. caroxy"e"tidase !.
&. cyclic !4P de"endent "rotein +inase.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #) $inding of sustrate alters the conformation of the en1yme.
*eedac+ &)
5=. :verall totally anaeroic glycolysis "rovides less !TP than aeroic glycolysis ecause
!. less or no 0!#, is recovered during anaeroic glycolysis.
$. less 0!# is availale under anaeroic conditions. so glycolysis cannot continue.
%. lactate "roduced anaeroically inhiits "hos"hofructo+inase51.
#. lactate is not a sustrate for "yruvate dehydrogenase.
&. more than one of the aove is correct.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) The 0!#, is oxidi1ed to 0!#< y the conversion of "yruvate to lactate. so that the 0!#<
can e used for another round of glycolysis. The 0!#, is thus not availale for oxidative "hos"horylation.
*eedac+ $) 'ee !.
*eedac+ %) %itrate and !TP inhiit P*751.
*eedac+ #) True. ut it is the 0!#, that is im"ortant ecause it and *!#,3 transfer reducing "otential
to electron trans"ort. The T%! cycle only ma+es one GTP (ithout electron trans"ort.
*eedac+ &)
5>. The "rotective mechanism "reventing accumulation of ammonia in most tissues resides in (hich
en1yme;
!. as"artate aminotransferase -G:T2
$. glutaminase
%. gamma5glutamyl trans"e"tidase
#. glutamine synthetase
&. argininosuccinate synthetase
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #) Glutamine removes ammonia from tissues and trans"orts it to the liver for further
metaolism to urea.
*eedac+ &)
5A. %hanges in en1yme activities I0 'ITL often involve Eallosteric effects.E This regulation most commonly
is seen through changes in
!. Mmax.
$. 7m.
%. en1yme concentration.
#. "hos"horylation of reactive serines.
&. Mmax and 7m.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $) !llosteric modifiers most often change an en1ymeIs affinity for sustrateH high 7m indicates
lo( affinity.
*eedac+ %)
*eedac+ #)
*eedac+ &)
6@. Phos"hofructo+inase53 (as descried as a EtandemE or ifunctional en1yme. This means that
!. this en1yme can cataly1e more than one reaction.
$. this en1yme hydroly1es fructose51.65di"hos"hate and may also cataly1e the formation of this same
com"ound.
%. this en1yme has Egrou"E or EclassE s"ecificity.
#. this en1yme cataly1es the formation of fructose51.65di"hos"hate.
&. this en1yme cataly1ed the hydrolysis of fructose53.65di"hos"hate to give fructose535"hos"hate.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) It has t(o "arts) the +inase that cataly1es "hos"horylation and the "hos"hatase that
cataly1es de"hos"horylation.
*eedac+ $) ,ydrolysis and "hos"horylation that converts et(een fructose53.65is"hos"hate and
fructose565"hos"hate.
*eedac+ %)
*eedac+ #) 'ee $.
*eedac+ &) 'ee $.
61. !n im"ortant source of reducing "o(er for iosynthesis is the reaction cataly1ed y
!. malate dehydrogenase.
$. "yruvate dehydrogenase.
%. acyl5%o! dehydrogenase.
#. glycerol585"hos"hate dehydrogenase.
&. glucose565"hos"hate dehydrogenase.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &) Part of the ,4P "ath(ay that "roduces 0!#P, (hich is needed for iosynthesis of fatty
acids. steroids. etc.
63. !rgininosuccinate is an intermediate in the de novo iosynthesis of
!. heme.
$. adenosine mono"hos"hate.
%. uridine mono"hos"hate.
#. creatine.
&. urea.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &) arininosuccinate 5556 fumarate < arginine 5556 urea < ornithine
68. 9hat is the net yield of 0!#, (hen glucose 65"hos"hate is converted to lactate y anaeroic
glycolysis;
!. @
$. 1
%. 3
#. 8
&. 4
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) Glyceraldehyde585"hos"hate dehydrogenase "roduces 0!#, and lactate dehydrogenase
oxidi1es 0!#, to 0!#<.
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
64. !n International Lnit -IL2 is that quantity of en1yme (hich can convert sustrate to "roduct at a rate
of
!. 1 micromoleJmin.
$. 1 micromoleJsec.
%. 1 millimoleJmin.
#. 1 millimoleJsec.
&. 1 nanomoleJsec.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
65. You have Dust finished a meal containing 1@@ grams of carohydrate. 5@ grams of fat and 35 grams of
"rotein. ,o( many +ilocalories did you consume;
!. 85@
$. 65@
%. A5@
#. 135@
&. 155@
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) 1@@g car -4 %alJg2 < 5@g fat -A %alJg2 < 35g "rotein -4 %alJg2 P A5@ %al or +cal.
*eedac+ #)
*eedac+ &)
66. !ll of the follo(ing can increase the activity of muscle glycogen "hos"horylase EE -de"endent2 exce"t
for
!. e"ine"hrine.
$. cyclic !4P.
%. glycogen "hos"horylase +inase.
#. 5Q5adenosine mono"hos"hate -!4P2.
&. glucagon.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &) Glucagon does not effect muscle.
6=. The maDor rate5limiting ste" of glycolysis in liver cells is
!. the conversion of glucose to glucose 65"hos"hate.
$. the conversion of glucose 65"hos"hate to fructose 65"hos"hate.
%. the conversion of fructose 65"hos"hate to fructose 1.65is"hos"hate.
#. the aldolase reaction.
&. none of the aove.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) The committed ste" cataly1ed y P*751.
*eedac+ #)
*eedac+ &)
6>. ! ne( en1yme has een isolated and sho(n to have a native molecular (eight of 34@.@@. In the
"resence of >4 urea the molecular (eight of the en1yme (as estimated to e 13@.@@@. 9hen eta5
merca"toethanol (as added to the urea system. the molecular (eight (as found to e 6@.@@@. 9hich of
the follo(ing est descries the suunit or "oly"e"tide structure of the en1yme;
!. The en1yme consists of t(o suunits (ith no interchain disulfide ridges.
$. The en1yme consists of four "oly"e"tide chains (ith no interchain disulfide ridges.
%. The en1yme consists of t(o "oly"e"tide chains (ith disulfide ridges.
#. The en1yme consists of four "oly"e"tide chains interconnected y disulfide ridges.
&. The en1yme consists of t(o "airs of "oly"e"tide chains (ith each "air interconnected y a disulfide
ridge.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &) Lrea disru"ts the noncovalent interactions et(een the 3 suunits and eta5merca"toethanol
disru"ts the disulfide onds in each suunit.
6A. !ssume that the 'T!0#!/# */&& &0&/GY change for the reaction)
!TP 5556 !#P < Pi
is 5=.@ %alJmole. 9hat is the est estimate of the EactualE free energy change (hen the follo(ing
concentrations exist)
N!TP P 1x1@54O. N!#P P 1x1@55O. and NPi P 1x1@54O;
Lse / P 3.@ calJmole 7C. and T P 8@@ 7C.
!. 5=.8 %al
$. 51@.@ %al
%. 51@.8 %al
#. 513.8 %al
&. 518.A %al
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &) G P Go < 3.8/T log 7 G P 5=@@@ cal < 3.8-32-8@@2 log-1@54 ? 1@55J1@542 G P 518A@@ cal or
518.A %al
=@. 9hich citric acid cycle intermediate hel"s to regulate the rate of glycolysis y directly influencing the
activity of "hos"hofructo+inase;
!. %itrate
$. 'uccinate
%. !l"ha5+etoglutarate
#. :xaloacetate
&. 4alate
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) Inhiits P*751.
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
=1. 9hich "rimers (ill am"lify my favorite gene if it is in the context elo(; 5Q5GGT!%!GT%54Y *!M:/IT&
G&0&5%T!G!T%!T58Q
!. 5Q5G!%TGT!%% and 5Q5%T!G!T%!T
$. 5Q5GGT!%!GT% and 5Q5!TG!T%T!G
%. 5Q5GGT!%!GT% and 5Q5%T!G!T%!T
#. 5Q5G!%TGT!%% and 5Q5!TG!T%T!G
&. 5Q5GGT!%!GT% and 5Q5G!%TGT!%%
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) $oth "rimers "oint a(ay from the target.
*eedac+ $) Yes. these anneal to the sequences flan+ing the target and are oriented (ith their 8I ends
to(ards the target.
*eedac+ %) The first "rimer is correct. ut the second one "oints a(ay from the target.
*eedac+ #) $oth "rimers "oint the same (ay. (ith one "ointing a(ay from the target.
*eedac+ &) The first "rimer is correct. ut the second one is nonsense. it is com"lementary to the second
flan+ ut "arallel.
=3. The caron atom in urea synthesi1ed in the liver arises most directly from
!. as"artate.
$. %:3.
%. fumarate.
#. ornithine.
&. glutamate.
'ho( ans(er
%orrect !ns(er) $
*eedac+ $) The %:3 comes into the urea cycle through the synthesis of caramoyl "hos"hate.
*eedac+ %)
*eedac+ #)
*eedac+ &)
=8. Phos"hocreatine is im"ortant in metaolism ecause it
!. is a com"ound formed y oxidative "hos"horylation (hich can transfer a "hos"hate grou" to !#P.
$. serves in synthetic reactions as the source of the "hos"hate grou"s of %#P5choline.
%. is formed y sustrate5level "hos"horylation and irreversily transfers a "hos"hate grou" to !#P and
forms creatinine.
#. reacts (ith !#P to give !TP and creatine.
&. is the source of a nitrogen and the caron atoms of urea.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) Phos"hocreatine is sustrate level "hos"orylation not oxidative "hos"horylation.
*eedac+ $)
*eedac+ %) The reaction is reversile.
*eedac+ #) Phos"hocreatine is a tem"orary storage form of !TP in muscle.
*eedac+ &)
=4. #0! sequencing de"ends on generating a set of molecules that terminate at every "ossile "osition.
This is done y sto""ing the synthesis
!. using modified nucleotides lac+ing the 8Q hydroxyl grou".
$. using a #0! "olymerase "urified from a thermo"hilic organism.
%. using modified nucleotides "hos"horylated at the 5Q hydroxyl.
#. using modified nucleotides (ith deaminated ases.
&. using a non5"rocessive #0! "olymerase.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) Yes. the 8I hydroxyl is needed for elongation so removing it causes termination
*eedac+ $) This can e done. ut does not contriute to the mechanism of chain termination
*eedac+ %) 0o. normal nucleotides have 5I "hos"hates
*eedac+ #) 0o. this (ould Dust ma+e damaged #0!. it (ould not terminate the elongation.
*eedac+ &) 0o. this (ould Dust ma+e short "roducts. it (ould not allo( s"ecific termination.
=5. &ach of the follo(ing may e used to estimate the molecular (eight of a "rotein &?%&PT
!. sucrose density gradient centrifugation.
$. ion exchange chromatogra"hy.
%. '#' -sodium dodecyl sulfate2 gel electro"horesis.
#. gel filtration chromatogra"hy.
&. sedimentation and diffusion measurements.
'ho( ans(er
%orrect !ns(er) $
*eedac+ $) 'e"arates molecules ased on charge differences.
*eedac+ %)
*eedac+ #)
*eedac+ &)
=6. !$ arises from a ==@ amino acid memrane "rotein called !PP -amyloid "recursor "rotein2. !PP is
mostly "rocessed y al"ha and gamma secretases to yield. among other fragments. a small "e"tide "8
that causes little harm. &nhanced "rocessing y eta5secretase and gamma5secretase generates the 4@ or
43 residue !$ "e"tide that results in !l1heimer amyloid de"osits. !PP s"ans the li"id ilayer et(een
residues 6=1 and ==@. and the last fe( residues of !$ are in the ilayer. *rom (hat you +no( aout
memrane "roteins (hich one of the follo(ing sequences identifies the last 5 amino acids in the 43
residue !$ "e"tide.
!. !s"5!la5Glu5Phe5!rg
$. Gly5Mal5Mal5Ile5!la
%. ,is5!s"5'er5Gly5Tyr
#. Bys5Mal5,is5,is5Gln
&. Glu5!s"5Mal5Gly5'er
'ho( ans(er
%orrect !ns(er) $
*eedac+ $) $ecause the last fe( residues of the !$ "e"tide are in the memrane they need to y
hydro"hoic -non5"olar2.
*eedac+ %)
*eedac+ #)
*eedac+ &)
==. The glycerol "hos"hate shuttle
!. results in "roduction of dihydroxyacetone "hos"hate in the matrix of mitochondria.
$. transfers electrons from cytosolic 0!#, to the res"iratory chain of mitochondria.
%. inhiits glycolysis.
#. su""orts "hos"horylation of three moles of !#P "er mole of cytosolic 0!#, oxidi1ed.
&. uses 85"hos"hoglyceric acid as a sustrate.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) #,!P is transferred out of the mitochondria.
*eedac+ $)
*eedac+ %)
*eedac+ #) Transfers 0!#, reducing "otential into the mitochondria as *!#,3. (hich su""orts the
"hos"horylation of 3!TP.
*eedac+ &)
=>. 9hen modifying the 'outhern lot "rocedure to do a 0orthern lot. you (ould (ant to avoid the ste"
in (hich
!. the nucleic acid molecules are se"arated y electro"horesis in agarose.
$. the gel is soa+ed in sodium hydroxide to denature the nucleic acids.
%. the nucleic acids are transferred to a solid matrix y ca"illary action.
#. a denatured "roe is added to the solid matrix and incuated at 65C %.
&. "roe that has hyridi1ed to the immoili1ed nucleic acids is detected.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) 0o. this is necessary to gather si1e information
*eedac+ $) Yes. /0! is sensitive to hydrolysis in solutions (ith high ", values. so this (ould tend to
destroy the /0! that is eing tested in a 0orthern.
*eedac+ %) 0o. this is the same in 'outherns and 0ortherns.
*eedac+ #) 0o. this is the same in 'outherns and 0ortherns.
*eedac+ &) 0o. this is the same in 'outherns and 0ortherns.
=A. Lrea is the "roduct of an en1yme in liver (hich cataly1es the hydrolysis of
!. caramoyl "hos"hate.
$. citrulline.
%. ornithine.
#. argininosuccinate.
&. arginine.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &) caramoyl "hos"hate < ornithine 5556 citrulline < as"artate 5556 argininosuccinate 5556
arginine 5556 urea
>@. *rom (hat you +no( aout "rotein chemistry. (hich "e"tide migrates fastest to the cathode -or
negative charged electrode2 at ", 6.@.
!. !s"5!la5Glu5Phe5!rg
$. Gly5Mal5Mal5Ile5!la
%. ,is5!s"5'er5Gly5Tyr
#. Bys5Mal5,is5,is5Gln
&. Glu5!s"5Mal5Gly5'er
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) 51. @. 51. @. <1 P 51
*eedac+ $) @. @. @. @. @
*eedac+ %) <1. 51. @. @. @ P @
*eedac+ #) <1. @. <1. <1. @ P <8
*eedac+ &) 51. 51. @. @. @ P 53 This "e"tide (ould migrate fastest to(ard the anode.
>1. 9hich of the follo(ing is a sustrate for /0! synthesis. ut not #0! synthesis;
!. adenosine tri"hos"hate -!TP2
$. deoxyuridine tri"hos"hate -dLTP2
%. guanosine55Q. 5Q5guanosine tri"hos"hate -G"""G2
#. cyclic adenosine mono"hos"hate -c!4P2
&. "seudouridine tri"hos"hate -"siTP2
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) Yes. this a rionucleoside tri"hos"hate suitale for synthesis of /0!.
*eedac+ $) 0o. d0TPs are not found in /0!
*eedac+ %) 0o. this is not a sustrate for an /0! "olymerase.
*eedac+ #) 0o. this has no free hydroxyl to "artici"ate in the "olymeri1ation reaction.
*eedac+ &) 0o. this is not a standard 0TP used y /0! "olymerase.
>3. !mmonium ion in the urine arises "rimarily from
!. the action of glutamate dehydrogenase in the +idney.
$. the action of glutaminase in the +idney on the amide nitrogen of glutamine.
%. the action of glutamine aminotransferase in the +idney.
#. the action of glutaminase in the +idney on the al"ha5amino grou" of glutamine.
&. the action of as"araginase in the +idney.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $) In the "roximal tuules glutamine is deaminated to glutamate and ammonia.
*eedac+ %)
*eedac+ #)
*eedac+ &)
>8. The com"ound (hich acce"ts a t(o5caron fragment from acetyl5%o! to initiate the citric acid cycle is
!. oxalosuccinate.
$. oxalate.
%. oxaloacetate.
#. oxytocin.
&. oxyutyrate.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) acetyl %o! < oxaloacetate 5556 citrate
*eedac+ #)
*eedac+ &)
>4. 7etosis may develo" as a result of (hich of the circumstances elo(;
!. glucose synthesis from fatty acids during glucose de"rivation
$. acute attac+ of gout
%. carnitine transferase I deficiency
#. hy"erglycemia
&. fat moili1ation to su""ort gluconeogenesis
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &) 7etone odies are "roduced ecause more acetyl %o! is derived from fatty acid oxidation
than can e used in T%! cycle.
>5. The al"ha5amino grou"s on most mammalian "roteins are acetylated. That is they have the structure)
%,85%-P:250,5%5"e"tide ,o(ever. the al"ha5amino grou"s on al"ha5 and eta5 hemogloin suunits are
not acetylated. Their acetylation (ould li+ely)
!. "revent inding of "rotons to ,
$. "revent $PG inding to ,
%. /educe %:3 elimination y the lungs
#. ! < %
&. $ < %
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) Protons ind to al"ha5amino grou"s of the al"ha chains and to caroxyl terminal ,is residues
of the eta chains. The eta chains (ould still ind "rotons.
*eedac+ $) Yes. the terminal amino grou"s of the eta chains aid in onding $PG.
*eedac+ %) !l"ha5amino grou"s react (ith %:3) 50,3 < %:3 5556 0,%::5 < ,<
*eedac+ #)
*eedac+ &)
>6. ! "erson (ith ?eroderma "igmentosum
!. is missing the en1yme that reverses thymine dimers
$. is sensitive to ultraviolet radiation -LM2
%. is sensitive "rimarily to ioni1ing radiation -x5rays2
#. is "rone to cancers and should e treated "ro"hylactically (ith radiation thera"y
&. is missing one of the = genes that encode ty"e II to"oisomerases
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) 0o. that is called "hotolyase. and has not een found in humans.
*eedac+ %) 0o. they are sensitive to LM
*eedac+ #) 0o. due to the defect in damage re"air. radiation thera"y is not indicated.
*eedac+ &) There are = classes of ?P. ut none are +no(n to have a defect in a ty"e II to"oisomerase.
>=. ! "erson regularly eating a high "rotein diet -diet 12 changes to diet 3 (hich contains adequate ut
sustantially less "rotein. !fter a "eriod of several days on diet 3. (hat (ill occur;
!. 0itrogen alance (ill e "ositive.
$. 0itrogen alance (ill e negative.
%. #aily out"ut of urea (ill increase over that (hile on diet 1.
#. #aily out"ut of urea (ill decrease elo( that (hile on diet 1.
&. T(o of the aove are true.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #) %onsumed amino acids are used for "rotein re"lacement and excess amino acids are
cataoli1ed for energy. There is no real storage form of amino acids. $ecause diet 3 has less "rotein
inta+e. there is less excess "rotein to cataoli1e.
*eedac+ &)
>>. The three stranded collagen su"erhelix is characteri1ed y the follo(ing "ro"erties &?%&PT )
!. Glycine is "resent every third residue
$. ,5onds are "arallel to the helix axis
%. 'ome lysines and "rolines are hydroxylated
#. 'ugars can e attached to hydroxylated lysine residues
&. 0o exce"tions
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $) The ,5onds occur t(een the three strands and are more "er"endicular to the axis.
*eedac+ %)
*eedac+ #)
*eedac+ &)
>A. The #0! that is co"ied y the t(o re"lication for+s traveling in o""osite directions from a common site
of initiation is called)
!. a du"lex
$. an origin
%. a attery
#. a re"licon
&. a trans"oson
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) 0o. a du"lex is the name for the t(o stranded form of #0!
*eedac+ $) 0o. the origin is the site of initiation itself.
*eedac+ %) 0o. a attery is a grou" of adDacent origins that fire simultaneously
*eedac+ #)
*eedac+ &) 0o. this is a "iece of #0! ca"ale of moving to other sites in the genome.
A@. Bysosomal en1ymes are often maximally active at ", 5.@ or less. In many cases. they are inactive at
", =.@ (hich ma+es some iological sense in that lysosomal ru"ture (ould e lethal if the released
"roteases and nucleases (ere significantly active at cytosolic ", -R =.@2. The amino acid / grou" most
affected y a change in ", from 5 to = is)
!. arginine
$. as"artate
%. cysteine
#. histidine
&. lysine
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #) ,istidineIs imida1ole ring readily acce"ts or donates "rotons. "7a P 6.5.
*eedac+ &)
A1. The "rocessivity of #0! "olymerases
!. increases in the "resence of ligases
$. decreases in the "resence of helicases
%. increases in the "resence of single strand inding "roteins
#. increases in the "resence of :+a1a+i factors
&. decreases in the "resence of clam" "roteins
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) 0o. ligases seal nic+s in #0!. they do not influence the tendency to move for(ard or fall off.
*eedac+ $) 'ome helicases affect "olymerase "rocessivity. ut they increase this "ro"erty.
*eedac+ %) Yes. ''$s straighten the tem"late and increase oth the rate and "rocessivity of #0!
"olymerases
*eedac+ #) 0o. there is no such thing as an :+a1a+i factor. and the si1e of :+a1a+i fragments are the
result. rather than the cause. of "rocessivity changes.
*eedac+ &) %lam" "roteins increase the "rocessivity of #0! "olymerases.
A3. 4c!rdleQs disease is due to a muscle
!. derancher en1yme defect.
$. glucosidase defect.
%. "hos"hofructo+inase defect.
#. "hos"horylase asence.
&. "hos"hohexose isomerase deficiency.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) %oriIs #isease of !ndersenIs #isease
*eedac+ $) Pom"eIs #isease
*eedac+ %) Glycogen storage disease MII
*eedac+ #) %annot degrade glycogenH limited aility to "erform strenuous exercise.
*eedac+ &)
A8. The follo(ing secondary structures can e classified according to the length of. say ten residues. in the
s"ecific conformation. *rom longest to shortest they are)
!. eta strand. collagen strand. al"ha5helix. "i5helix
$. %ollagen strand. eta strand. al"ha5helix. "i5helix
%. al"ha5helix. eta strand. "i5helix. collagen strand
#. al"ha5helix. "i5helix. eta strand. collagen strand
&. %ollagen strand. al"ha5helix. eta strand. "i5helix
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
A4. ! acterial culture gro(n for many generations in a EheavyE -1502medium (as transferred to a ElightE
-1502 medium. !fter the #0! had een co"ied 8 times in light medium. (hat (ould e the relative
distriution of #0! containing t(o light strands -BB2. one heavy and one light strand -,B2. and t(o heavy
strands -,,2;
!. 3 ,,)3 BB
$. 1 ,,)1,B)6 BB
%. @ ,,)1 ,B) =BB
#. @ ,,)1 ,B) 8BB
&. 1 ,,)3 ,B) 1BB
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) !fter 1 round the #0! is all ,B. after 3 it is 1 ,B)1 BB. and after 8 it is 1 ,B)8 BB. There is no
,, after the first round.
*eedac+ $) !fter 1 round the #0! is all ,B. after 3 it is 1 ,B)1 BB. and after 8 it is 1 ,B)8 BB. There is no
*eedac+ %) !fter 1 round the #0! is all ,B. after 3 it is 1 ,B)1 BB. and after 8 it is 1 ,B)8 BB. This ratio
(ould result after 4 rounds
*eedac+ #) !fter 1 round the #0! is all ,B. after 3 it is 1 ,B)1 BB. and after 8 it is 1 ,B)8 BB.
*eedac+ &) !fter 1 round the #0! is all ,B. after 3 it is 1 ,B)1 BB. and after 8 it is 1 ,B)8 BB. There is no
A5. 4utations can alter "rotein structure and lead to devastating diseases. %onsider the follo(ing amino
acid changes) 1. Tyr to Phe 3. !s" to !sn 8. Ile to !rg 4. !rg to Bys 5. ,is to !sn 6. Tr" to Gly =. !la to
Pro 9hich change is most li+ely to alter the asorance of a "rotein at 3>@ nm;
!. 3
$. 8
%. 4
#. 5
&. 6
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &) Glycine is unique in eing o"tically inactive. and try"to"han is aromatic.
A6. In methylation5directed mismatch re"air in acteria
!. 4utB inds to mismatches in du"lex #0!
$. The methylated strand is Dudged to e the older strand
%. 4utB inds to methylated #0! strands
#. :ne mismatched ase is excised leaving a single nucleotide ga" to re"air
&. /ec! ma+es an incision only at hemimethylated sites
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) 0o. 4ut' has this activity. the activity is 4utB remains "oorly understood.
*eedac+ $) Yes. since ne(ly synthesi1ed #0! does not have this "ost5synthetic modification. the
methylated strand is older.
*eedac+ %) 0o. 4ut, seems to have this "ro"erty. the activity is 4utB remains "oorly understood.
*eedac+ #) 0o. this (ould e ase5excision re"air.
*eedac+ &) !n incision is made at hemi5methylated sites. ut y 4ut,. not /ec!
A=. 4utations can alter "rotein structure and lead to devastating diseases. %onsider the follo(ing amino
Pro 9hich change is most li+ely to disru"t the folding of a gloular "rotein;
!. 1
$. 3
%. 8
#. 4
&. 5
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) $oth are aromatic.
*eedac+ $) :nly one grou" is different and oth are "olar.
*eedac+ %) Ile is non5"olar. !rg is very "olar and its / grou" is a""roximately t(ice as long as Ile.
*eedac+ #) $oth have long / grou"s and oth are ases.
*eedac+ &) $oth are "olar.
A>. !ll of the follo(ing statements concerning eu+aryotic #0! re"lication are true &?%&PT
!. single5strand inding "roteins coat some #0! intermediates in re"lication
$. re"lication of half of the #0! chains occurs in short discontinuous "ieces
%. helicases un(ind the "arental strands for the "olymerases
#. a single ty"e of #0! "olymerase acts on oth leading and lagging strands
&. ring5sha"ed clam" "roteins "romote high "rocessivity of #0! "olymerase
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) ''$s are needed for all "hases of #0! metaolism. including re"lication.
*eedac+ $) This is true. descriing the synthesis of :+a1a+i fragments on the lagging strand.
*eedac+ %) 9hile the "recise identity of the eu+aryotic re"licative helicase is not +no(n. this is very
li+ely to e true given the rate of re"lication for+ movement.
*eedac+ #) This is unli+ely to e true since oth Pol al"ha and Pol delta seem to e needed for
eu+aryotic re"lication. although their exact roles remain un+no(n.
*eedac+ &) This is true. the clam" is called P%0!.
AA. 'ustrate 7m S1 3.5 S3 13.@ S8 83.@ %om"arison of the res"ective 7m values for the hydrolysis of
the "e"tide ond of sustrates 158 y chymotry"sin sho(s that
!. The Mmax of sustrate S1 must e greater than that for S3 or S8.
$. The Mmax for sustrate S8 must e greater than that for S1 or S3.
%. ! lo(er concentration of S8 (ill e needed to attain Mmax.
#. ! lo(er concentration of S1 (ill e needed to attain Mmax.
&. 'ustrate S8 has the highest affinity for the active stie of chymotry"sin.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) The 7m tells us the concentration of sustrate needed to reach 1J3 Mmax for a "articular
en1yme. ut "rovides no com"arison for the actual velocities.
*eedac+ $) 'ee !.
*eedac+ %) 'ince 7m. (hich tells us the concentration needed to reach 1J3 Mmax. is highest for S8. S8
must need the highest concentration to reach full Mmax.
*eedac+ #) 'ee %.
*eedac+ &) ,igher 7m indicates less affinity of the en1yme for the sustrate.
1@@. Ioni1ing radiation is ca"ale of "roducing genetic mutations y
!. !ltering ases so that they form different ase "air interactions
$. %ausing deletions of #0! sequences
%. %ausing inversions of #0! sequences
#. %ausing translocations of one "art of a chromosome onto another
&. !5# are all correct.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) True. ut so are all of the choices. so the ans(er is &
*eedac+ $) True. ut so are all of the choices. so the ans(er is &
*eedac+ %) True. ut so are all of the choices. so the ans(er is &
*eedac+ #) True. ut so are all of the choices. so the ans(er is &
*eedac+ &)
1@1. 9hich of the follo(ing cases re"resents a metaolically im"ortant control;
!. 'ustrate oxidation in mitochondria is enhanced y elevated !TP levels.
$. The activity of liver hexo+inase is stimulated y high levels of its "roduct. glucose 65"hos"hate.
%. !cetyl5%o! inhiits "yruvate caroxylase in the liver.
#. Phos"hofructo+inase -P*72 is inhiited y high levels of its sustrate. 4g!TP.
&. Glucagon stimulates he"atic glycogen synthase.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) Increased !TP shuts do(n en1ymes of glycolysis and T%! cycle. so oxidation is decreased.
*eedac+ $) ,exo+inase is inhiited y glucose565"hos"hate.
*eedac+ %) The activity of "yruvate caroxylase requires acetyl %o!.
*eedac+ #) !TP and citrate inhiit P*751. 7inases require divalent metal ions such as 4g3< or 4n3< for
activity. The divalent ions com"lex (ith !TP.
*eedac+ &) Glucagon sto"s glycogen synthesis and "romotes glycogen degradation.
1@3. 4utations can alter "rotein structure and lead to devastating diseases. %onsider the follo(ing amino
Pro 9hich change is most li+ely to inactivate an en1yme (ithout greatly altering its conformation;
!. 3
$. 8
%. 4
#. 5
&. 6
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) !s" and !sn are structurally very similar. ut !s" is an acid. and usually charged at
"hysiological ",.
*eedac+ $) 9ould greatly affect conformation.
*eedac+ %) $oth are asic and have fairly large / grou"s. so there (ould li+ely e little affect.
*eedac+ #) Bess li+ely than ans(er ! -32. ut this (as acce"ted as correct (hen this exam (as
administered. ,is is a ase and !sn is not. and they are structurally quite different.
*eedac+ &) 'tructrually very different. (ould affect conformation.
1@8. %ells lac+ing "58 are anormal ecause they
!. lac+ en1ymes needed for ase excision re"air
$. fail to enter ' "hase if their #0! is damaged
%. arrest in mitosis in the "resence of high levels of caffeine
#. fail to die after ex"osure to lo( levels of #0! damage
&. ! and % are oth correct
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) 0o. $&/ is normal in "58 mutants
*eedac+ $) 0o. this (ould e the normal res"onse. not an anormal one.
*eedac+ %) 0o. this (ould descrie an overactive chec+"oint. not the underactive one found in "58
mutants
*eedac+ #) Yes. cells (ith #0! damage undergo a"o"tosis. ut this res"onse requires "58.
*eedac+ &) 0o. neither ! nor % are correct.
1@4. The follo(ing are general "ro"erties of firous "roteins &?%&PT)
!. They serve structural roles
$. They involve extended conformations of "oly"e"tide chains
%. They are located outside cells
#. They are often com"osed of intert(ined "oly"e"tide chains
&. 0o exce"tions
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) Proteins ma+e u" cellular com"onentsH firous "roteins ma+e u" cytos+eletal elements.
*eedac+ #)
*eedac+ &)
1@5. Telomeres get shorter in somatic tissues as the individual ages. therefore
!. mice have long telomeres ecause th
ey have a short life s"an
$. aging correlates negatively (ith telomere length
%. telomerase must e "resent for cells to age
#. loc+ing telomerase (ould sto" cells from aging
&. enhancing telomerase (ould sto" cells from aging
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) 0o. this does not follo( from the oservation. and is in fact the o""osite of (hat (ould e
ex"ected.
*eedac+ $) Yes. this is Dust a restatement of the oservation.
*eedac+ %) 0o. this is not a logical conclusion to the oservation
*eedac+ #) 0o. this is not a logical conclusion. and in fact is o""osite of the ex"ectation.
*eedac+ &) 0o. this might e true. ut is not necessarily so. and is unli+ely to e correct in any com"lete
sense.
1@6. !ll of the follo(ing statements a""ly to the electron trans"ort chain &?%&PT (hich one;
!. The cytochromes of the system are emedded in the inner mitochondrial memrane.
$. !n uncou"ler sto"s the flo( of electrons do(n the res"iratory chain.
%. ! maximum of 8 !TP is generated y the reoxidation of one 0!#, through oxidative "hos"horylation.
#. %ytochrome oxidase is a +ey com"onent of this system.
&. The rate of electron trans"ort is normally controlled y the concentration of mitochondrial !#P.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $) &lectron trans"ort still frunctions and "rotons are "um"ed to the intermemrane s"ace. ut
the uncou"ler allo(s the "rotons to y"ass the !TP synthase.
*eedac+ %)
*eedac+ #)
*eedac+ &) /es"iratory control.
1@=. Given this information. (hat technique-s2 (ould e least useful for determining (hether an
individualQs huntingtin "roteins contained extensions of 6@ additional glutamines.
!. Ion exchange chromatogra"hy
$. 0ative gel electro"horesis
%. '#'5P!G&
#. !mino acid analysis
&. ! and $
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) 'e"arates ased on charge. ut 6@ glutamines do not alter charge.
*eedac+ $) Proteins are se"arated ased on sha"e and charges. not y si1e differences.
*eedac+ %) '#' creates uniform charge density and allo(s se"artation ased on si1e difference.
*eedac+ #) 9ould sho( a higher "ercentage of glutamine. and the com"lete sequence could e
determined.
*eedac+ &)
1@>. $acteria use visile light to reverse "yrimidine dimer damage. 9hich of the follo(ing is an accurate
statement regarding this "rocess;
!. ! "yrimidine dimer asors a "hoton of the same (avelength that caused the damage and reverses the
reaction.
$. !n en1yme called "hotolyase ma+es t(o incisions in the #0! near a "yrimidine dimer. releasing the
damaged strand
%. #uring re"air. the damaged ases are removed and re"laced (ith ne(ly synthesi1ed material
#. Photolyase removes the damaged ases only. leaving aasic sites that are re"aired y other en1ymes
later.
&. Photolyase asors a "hoton of visile light and converts the energy to s"ecifically reverse the
"yrimidine dimeri1ation reaction
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) 0o. the en1yme asors the "hoton. and it is al(ays a different -longer. visile2 (avelength.
*eedac+ $) 0o. this descries nucleotide excision re"air. not reversal.
*eedac+ %) 0o. reversal involves re"air (ithout resynthesis
*eedac+ #) 0o. the ases are not removed. they are chemically returned to their original form
*eedac+ &)
1@A. The chemiosmotic hy"othesis suggests that the "otential energy of the electrons moving do(n the
mitochondrial electron trans"ort chain from a negative to a "ositive oxidation "otential is initially
conserved in the form of a
!. "roton gradient across the memrane.
$. a high energy "hos"hate ond.
%. a different conformational form of the electron carriers.
#. a "rotonated form of coen1yme T.
&. a reduced non5heme iron "rotein.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) The chemiosmotic hy"othesis ex"lains the lin+ et(een electron trans"ort and !TP synthesis.
(hich is the "roton gradient.
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
11@. 9hich technique (ould e the est for detecting the additional glutamines;
!. Ion exchange chromatogra"hy
$. 0ative gel electro"horesis
%. '#'5P!G&
#. !mino acid analysis
&. ! and $
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %) '#'5P!G& (ould tell us that the anormal "rotein is larger. ut not (hat amino acids (ere
added.
*eedac+ #) 9ith techniques such as &dman #egradation (e can rea+ off and analy1e one amino acid at
a time.
*eedac+ &)
111. 4utations caused y one of the follo(ing agents almost al(ays inactivate genes s"ecifying "rotein
"roducts. ut often do not affect the function of genes s"ecifying only stale /0! "roducts. 9hich agent is
it;
!. LM light
$. cis5"latin
%. intercalating agents
#. EmustardE gases
&. 55romouracil
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) 0o. LM light ty"ically causes single ase changes. (hich are as ad for "roteins as for /0!s
*eedac+ $) 0o. this is ty"ically a crosslin+er leading to doule5strand rea+s.
*eedac+ %) Yes. these cause insertions and deletions leading to frame5shifts that are much (orse for
:/*s than for /0!s
*eedac+ #) 0o. these are ty"ically a crosslin+ers leading to doule5strand rea+s.
*eedac+ &) 0o. this causes an enforced tautomeric shift leading to single ase changes.
113. 9hen e"ine"hrine inds to its rece"tor on s+eletal muscle. glycogenolysis is stimulated. The hormone
signal influences the activity of each of these en1ymes &?%&PT)
!. "hos"horylase.
$. adenylate cyclase.
%. "hos"horylase +inase a.
#. cyclic !4P5de"endent "rotein +inase.
&. deranching en1yme.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &) e"hine"hrine inds 5556 active adenylate cyclase 5556 increased c!4P 5556 active P7! 5556
active "hos"orylase +inase 5556 active glycogen "hos"horylase
118. !lthough theoretically "ossile ased on acce"tale angles. the "i5helix has not een oserved in real
"roteins ecause)
!. %aroxyl5amide ,5onds cannot form.
$. / grou"s lie aove one another.
%. ,5onds are too long.
#. Bac+ of favorale Man der 9aals interactions in the helix axis.
&. The "i5helix has een foundU
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #) The al"ha5helix has a radius that allo(s excellent van der 9aals attractions across the axis.
*eedac+ &)
114. In (hich disorder is mismatch re"air found to e defective;
!. !taxia telangiectasia
$. %oc+ayneQs 'yndrome
%. $loomQs syndrome
#. ,ereditary non5"oly"osis colon cancer -,0P%%2
&. ?eroderma "igmentosum -?P2
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) 0o. the !T4 gene defective in this disorder a""ears to e a chec+"oint gene.
*eedac+ $) This is associated (ith re"air defects. ut not mismatch re"air.
*eedac+ %) This is associated (ith re"air defects. ut not mismatch re"air.
*eedac+ #) Yes. these disorders are associated (ith mutations in homologs of the acterial 4ut' and
4utB genes.
*eedac+ &) This is associated (ith re"air defects. ut not mismatch re"air.
115. 9hich statement aout gluconeogenesis is correct;
!. The acetate grou" of acetyl5%o! is used for the net synthesis of glucose.
$. It occurs "rimarily in s+eletal muscle.
%. It occurs through reversal of the reactions of glycolysis.
#. Bactate and alanine can oth serve as sustrates.
&. !TP is not required.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $) Primarily in the liver and some in the +idney.
*eedac+ %) The irreversile reactions of glycolysis must e reversed y en1ymes unique to
gluconeogenesis.
*eedac+ #)
*eedac+ &) 4 !TP are required for each glucose "roduced.
116. !n en1yme affects the rate of a chemical reaction y
!. decreasing the free energy of the reaction.
$. increasing the free energy of the reaction.
%. lo(ering the energy of activation of the reaction.
#. raising the energy of activation of the reaction.
&. dis"lacing the equilirium constant.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
11=. %oncerning eta sheets the follo(ing statements are correct &?%&PT)
!. The eta strands can e "arallel or anti5"arallel.
$. The sheet can have an even or odd numer of strands.
%. The / grou"s of t(o consecutive amino acids are on o""osite sides of the sheet
#. Gly and Pro are not "resent.
&. !ll are correct.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) Parallel are usually found interiorly and anti"arallel on the surface of gloular "roteins.
*eedac+ $)
*eedac+ %) / grou"s are staggered.
*eedac+ #) Turns are enriched (ith gly and "ro. ut they can e found in a sheet. es"ecially gly.
*eedac+ &)
11>. The inhiition caused y a non5com"etitive inhiitor causes (hich of the follo(ing alteration-s2 in a
Bine(eaver5$ur+ "lot;
!. no change in the y5interce"t. ut a decrease in the x5interce"t
$. no change in the y5interce"t. ut an increase in the x5interce"t
%. no change in the y5interce"t. ut a decrease in the y5interce"t
#. no change in the x5interce"t. ut an increase in the y5interce"t
&. increases in oth the x5 and y5interce"ts
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #) 0on5com"etative inhiitors change Mmax. ut not 7m. The x5interce"t P 51J7m and the y5
interce"t P 1JMmax.
*eedac+ &)
11A. 9hat is the chemical difference et(een 0!# and 0!#P;
!. 0!#P has an additional "hos"horyl grou" at "osition S3Q on the "entose adDacent to adenine.
$. 0!# has a nicotinic acid moiety rather than nicotinamide.
%. 0!#P has an additional "hos"horyl grou" at "osition S8Q on the "entose adDacent to nicotinamide.
#. 0!#P has an additional "hos"horyl grou"ing as an acyl "hos"hate on the nicotinic acid moiety.
&. %hemically. they are identical.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $) $oth have nicotinamide.
*eedac+ %)
*eedac+ #)
*eedac+ &)
13@. Gluconeogenesis from lactate does not require activity of
!. aldolase.
%. glyceraldehyde 85"hos"hate dehydrogenase.
#. triose "hos"hate isomerase.
&. "hos"hoglycerate +inase.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $) P*751 cataly1es an irreversile reaction in glycolysisH fructose51.65is"hos"hatase is needed
in gluconeogenesis.
*eedac+ %)
*eedac+ #)
*eedac+ &)
131. #uring gluconeogenesis. (hich en1yme must e "resent in addition to the glycolytic en1ymes;
!. fructose 1.65is"hos"hate "hos"hatase
$. "hos"hofructo+inase
%. "yruvate +inase
#. "yruvate dehydrogenase
&. glyceraldehyde 85"hos"hate dehydrogenase
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) %arries out the reversal of the reaction cataly1ed y P*751 in glycolysis.
*eedac+ $) :nly used y glycolysis
*eedac+ %) :nly used y glycolysis
*eedac+ #) :nly used y glycolysis to T%!.
*eedac+ &) reversile.
133. In oxidative "hos"horylation. an uncou"ling agent causes (hich of the follo(ing;
!. $oth res"iration and "hos"horylation to decrease
$. Phos"horylation to remain constant and res"iration to decrease
%. /es"iration to increase and "hos"horylation to decrease
#. /es"iration and "hos"horylation to increase
&. 0one of the aove
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) &lectron trans"ort is functioning ut !TP synthesis is decreased. The decreased levels of !TP
stimulate glycolysis and T%! cycle to "roduce more 0!#, and *!#,3. (hich increase electron trans"ort.
*eedac+ #)
*eedac+ &)
138. The 0&T "roducts of anaeroic glycolysis are
!. "yruvate. 0!#. !TP.
$. lactate. 0!#. !TP.
%. lactate. !TP.
#. acetyl5%o!. 0!#,. !TP.
&. "yruvate. !TP.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) In aeroic glycolysis "yruvate. !TP. and 0!#, are "roduced. ut in anaeroic glycolysis
"yruvate < 0!#, 5556 lactate < 0!#.
*eedac+ #)
*eedac+ &)
134. Glycolysis is only "artially reversile ecause of energy arriers at the reactions cataly1ed y
!. hexo+inase. triose "hos"hate isomerase. and "yruvate +inase.
$. "hos"hofructo+inase. aldolase. and lactate dehydrogenase.
%. hexo+inase. "yruvate dehydrogenase. and "hos"hoenol"yruvate caroxy+inase.
#. hexo+inase. "hos"hofructo+inase. and "yruvate +inase.
&. hexo+inase. glyceraldehyde 85"hos"hate dehydrogenase. "yruvate +inase.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #) The 8 irreversile reactions of glycolysis (hich all involve !TP.
*eedac+ &)
135. The follo(ing "ro"erties are characteristic of all natural mammalian "roteins &?%&PT for
!. "lanar "e"tide onds.
$. defined amino acid sequence.
%. origins on riosomes.
#. com"osed of B5amino acids.
&. all are correct.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) #oule ond character.
*eedac+ $)
*eedac+ %) /iosomes synthesi1e "roteins.
*eedac+ #)
*eedac+ &)
136. !n Eallosteric effectorE of an en1yme (as defined as
!. a com"ound (hich increased the catalytic rate y inding to a site removed from the active site.
$. a com"ound (hich decreased the catalytic rate y inding to a site removed from the active site.
%. a com"ound (hich decreased the 7m for a sustrate.
#. a com"ound (hich changed the catalytic rate y inding to a site removed from the active site.
&. a com"ound (hich increased Mmax for an en1yme.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) The rate can e increased or decreased.
*eedac+ $) 'ee !
*eedac+ %) %hanges 7m y increasing or decreasing it.
*eedac+ #)
*eedac+ &) Lsually changes 7m.
13=. The cause of the most common form of galactosemia is
!. loss of lactase activity in the intestinal mucosa.
$. defective fructose 15"hos"hate aldolase.
%. inaility to convert L#P5galactose to L#P5glucose.
#. mil+ allergy.
&. defective uridylyltransferase.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) This can e a cause. ut is not the most common. The maDor dietary source of galactose is
lactose. (hich is ro+en do(n y lactase.
*eedac+ $) %auses fructose intolerance.
*eedac+ %) 'ee &.
*eedac+ #) 'ee !
*eedac+ &) %lassical galactosemiaH the follo(ing reaction does not occur) L#P5glucose < glactose515
"hos"hate 5556 L#P5galactose < glucose515"hos"hate.
13>. %ellular #0! and /0! synthesis are distinguished y (hich of the follo(ing;
!. release of the "roduct "olynucleotide from the tem"late
$. use of a #0! tem"late
%. selection of incoming nucleotides y 9atson5%ric+ ase "airing rules
#. release of "yro"hos"hate in the chemical ste" of synthesis
&. "olarity of synthesis of the ne( strand
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) In #0! synthesis the tem"late and the ne(ly synthesi1ed strand ecome ds#0!. /0! is
released from the #0! tem"late.
*eedac+ $) $oth /0! synthesis and #0! synthesis use a #0! tem"late
*eedac+ %) 9hile the nucleotides are different -T in #0!. L in /0!2. the next correct nucleotide is
chosen y ase5"airing in oth cases.
*eedac+ #) $oth /0! synthesis and #0! synthesis use nucleoside tri"hos"hates and release
"yro"hos"hate
*eedac+ &) $oth #0! and /0! are synthesi1ed 5I to 8I.
13A. The most common male human germ5line mutation is
!. ! to T transversions
$. ! to G transitions
%. % to ! transversions
#. % to T transitions
&. G to % transversions
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) The most common mutation in the male germ line is the % to T transition caused y
deamination of 55methyl cytosine.
*eedac+ $) The most common mutation in the male germ line is the % to T transition caused y
*eedac+ %) The most common mutation in the male germ line is the % to T transition caused y
*eedac+ #) The most common mutation in the male germ line is the % to T transition caused y
*eedac+ &) The most common mutation in the male germ line is the % to T transition caused y
18@. 9hich of follo(ing is 0:T true concerning $ form nucleic acids;
!. The #0! du"lex is destaili1ed y re"ulsion of the "hos"hates in the ac+ones.
$. There are aout 1@.5 " "er turn of the #0! helix.
%. The #0! du"lex is staili1ed y ase stac+ing interactions.
#. ,ydrogen onds form et(een ases on the t(o strands of the du"lex.
&. /0! does not ado"t the $ form ecause of the 8Q hydroxyl on the riose grou".
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) This is true. the charge re"ulsion is a significant force "ushing the strands a"art. and is the
asis of staili1ation y salts.
*eedac+ $) This is true for $5forms
*eedac+ %) This is true. and "rovides the main force staili1ing the du"lex
*eedac+ #) This is trueH ase "airing is largely due to these cross5strand interactions
*eedac+ &) The 3I hydroxyl is im"ortant for ! form. so #0! cannot ado"t this form. ut /0! has a 8I
hydroxyl so this res"onse is incorrect -ma+ing it the right ans(erU2
181. 9hich of the follo(ing "ro"erties of nucleotides does 0:T affect the structure of nucleic acids;
!. The ases are hydro"hoic.
$. The "hos"hates are negatively charged at neutral ",.
%. The ases can each form multi"le hydrogen onds
#. The ases asor ultraviolet light at a (avelength near 36@ nm.
&. The sugar grou" is highly (ater solule.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) This "rovides the main driving force for formation of the du"lex
*eedac+ $) The re"ulsion of the ac+ones is a significant force affecting the structure and staility of
du"lexes
*eedac+ %) The aility to form hydrogen onds is an im"ortant determinant of the s"ecificity of the
interaction et(een strands -the com"lementarity2.
*eedac+ #) This is true ut does not affect the structure of the du"lex
*eedac+ &) This "rovides soluility to nucleic acids
183. !cylovir is an analog of guanosine in (hich the riose ring is disru"ted. 9hich of the follo(ing
reasons ex"lains (hy this drug is useful for treating her"esvirus infections;
!. 0ormal cells are not "ermeale to the drug. ut infected cells are.
$. %ellular #0! "olymerase (ill not ind the analog. ut viral "olymerase (ill.
%. /ionucleotide reductase acts on acyclovir to form a suicide inhiitor of only the viral #0! "olymerase.
#. %ellular thymidine +inase (ill not act on the drug. ut the viral en1yme (ill.
&. Miral re"lication is faster than cellular re"lication. so the virus is more sensitive to any change in the
level of d0TPs.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) $oth +inds of cell are "ermeale to this drug.
*eedac+ $) The "olymerase doesnIt use acyclovir ecause it is not a tri"hos"hate. not ecause it doesnIt
ind.
*eedac+ %) /0/ does not act on acyclovirH it does not have a sugar moiety so it cannot have a 3I
hydroxyl.
*eedac+ #)
*eedac+ &) 0o. this is Dust confusing.
188. !dding high levels of thymidine to mammalian cells loc+s their "rogression through the cell cycle
ecause
!. these cells lac+ thymidine +inase.
$. rionucleotide reductase is inhiited y thymidine so no dTTP is "roduced.
%. #0! "olymerase is inhiited y thymidine.
#. the levels of d%TP are reduced due to the regulation of rionucleotide reductase.
&. this loc+s ty"e II to"oisomerases in a covalent intermediate (ith #0!.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) 0o. this is Dust made u"
*eedac+ $) 0o. ut this is closer. see #
*eedac+ %) 0o. this is Dust made u"
*eedac+ #)
*eedac+ &) 0o. this is Dust made u"
184. ,istones are usually
!. asic. and therefore negatively charged at neutral ",.
$. asic. and therefore "ositively charged at neutral ",.
%. acidic. and therefore negatively charged at neutral ",.
#. acidic. and therefore "ositively charged at neutral ",.
&. close to neutral. and therefore uncharged at neutral ",.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) $asic residues are "ositively charged at neutral ",
*eedac+ $)
*eedac+ %) !cidic residues are negatively charged at neutral ",. ut histones are rich in asic residues
*eedac+ #) !cidic residues are negatively charged at neutral ",. and histones are rich in asic residues
*eedac+ &) If neutral. there (ould e little charge. ut histones are rich in asic residues.
185. !s a result of ? chromosome inactivation
!. 4ales do not ex"ress the genes on the ? chromosome.
$. :ne co"y of the ? chromosome is inactivated no matter ho( many co"ies are "resent.
%. &x"ression of the genes on the Y chromosome is increased.
#. ! heterochromatic $arr ody forms and this structure is "ro"agated in susequent rounds of
re"lication.
&. The same ? chromosome is inactivated in all tissues. revealing recessive Esex5lin+edE mutations.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) 4ales have only one ? chromosome. inactivation affects one of the t(o co"ies found in
female cells
*eedac+ $) The o""osite is trueH only one co"y is left active no matter ho( many are "resent
*eedac+ %) The Y chromosome has fe( genes and their ex"ression is unaffected y ? inactivation. even
in cases (here a Y chromosome is found in a cell (ith t(o ? chromosomes (here inactivation occurs
*eedac+ #)
*eedac+ &) *emales are mosaics ecause different ? chromosomes are inactivated in different cell
lineages.
186. The "rocessivity of leading strand #0! "olymerases
!. increases (ith the addition of ligases.
$. decreases (ith the addition of helicases.
%. decreases (ith the addition of single strand inding "roteins.
#. increases (ith the addition of :+a1a+i factors.
&. increases (ith the addition of clam" "roteins.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) Bigase does not affect "rocessivity. it seals nic+s after re"lication or re"air is other(ise
com"lete
*eedac+ $) ,elicases un(ind the tem"late and enhance "rocessivity
*eedac+ %) ''$s straighten the tem"late and therefore enhance "rocessivity
*eedac+ #) There is no such thing.
*eedac+ &) %lam"s "revent "olymerases from leaving the "rimerJtem"late and so increase "rocessivity
18=. 7nots formed in #0! molecules are disentangled in eu+aryotic cells y
!. ty"e I to"oisomerases.
$. ty"e II to"oisomerases.
%. ty"e III to"oisomerases.
#. restriction endonucleases and #0! ligase.
&. #0! helicases and #0! ligase.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) Ty"e I to"o only rea+s one #0! strand and therefore cannot "erform the strand "assage
reaction required to untie +nots
*eedac+ $)
*eedac+ %) There is no such thing
*eedac+ #) /estriction en1ymes are only found in "ro+aryotes. and they donIt "erform this role their
either.
*eedac+ &) This (ould not (or+H helicases Dust un(ind they donIt rea+ the #0! ac+one
18>. !ll of the follo(ing statements are true (ith regard to #0! re"lication &?%&PT (hich one;
!. It involves a transient covalent lin+ et(een /0! and #0! chains.
$. /e"lication for+s move a(ay in $:T, directions from origins.
%. %hain gro(th occurs y addition at the 8Q end of ne( strands.
#. /ionucleoside tri"hos"hates are not used during re"lication.
&. %hain gro(th on one side of the re"lication for+ does not require continual action of "rimase.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) This is trueH the "rimers are /0! and are extended as #0!. "roducing the transient lin+.
*eedac+ $) This is true. origins give rise to t(o for+s that travel a"art.
*eedac+ %) This is true. nucleic acids are synthesi1ed 5I58I.
*eedac+ #) Yes. they are used in the synthesis of /0! "rimers. and also as an energy source for clam"
loading and helicase action.
*eedac+ &) This is true. the leading strand is synthesi1ed continuously and does not require re"eated
"riming -unli+e the lagging strand2.
18A. 'ince the genetic code is redundant. an im"ortant gene that encodes a "rotein (ill have its
!. #0! sequence accumulate changes more slo(ly than its amino acid sequence.
$. #0! sequence accumulate changes more ra"idly than its amino acid sequence.
%. #0! sequence accumulate changes at the same rate as its amino acid sequence.
#. m/0! accumulate changes more slo(ly than its amino acid sequence.
&. exons accumulate changes more ra"idly than introns.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) 'ince many #0! sequences can encode the same "rotein. the #0! sequence is under less
constraints and mutates more ra"idly than the "rotein sequence it encodes.
*eedac+ $) 'ince many #0! sequences can encode the same "rotein. the #0! sequence is under less
*eedac+ %) 'ince many #0! sequences can encode the same "rotein. the #0! sequence is under less
*eedac+ #) m/0! sequence matches the #0! and is only a tem"orary co"y. not a source of heritale
change.
*eedac+ &) &xons are under greater selective "ressure and therefore change more slo(ly than introns
14@. 4utations in #0!
!. are not im"ortant if they are in intron sequences.
$. are not im"ortant unless they occur in o"en reading frames.
%. al(ays have a negative im"act on the gene "roduct affected.
#. only affect single5co"y genes.
&. can change the translational reading frame of "roteins.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) This is often ut not al(ays true. In "articular. mutations in introns that affect the aility for
the introns to e s"liced affect gene function.
*eedac+ $) :/*s are the most ovious target for mutations that affect function. ut since flan+ing
regions alter the ex"ression of the :/* and the s"licing "atterns of messages. these sequences are also
im"ortant targets.
*eedac+ %) &volution is the "rocess of the slo( accumulation of eneficial mutations
*eedac+ #) 4utations occur at random and affect all genes. Phenoty"es are more li+ely to e oserved in
single co"y genes. ut that (asnIt the question.
*eedac+ &) These are called frameshifts.
141. Lltraviolet light damages cells most seriously y
!. causing doule strand rea+s in #0!.
$. altering the secondary structure of /0! molecules.
%. forming dimers et(een "yrimidines stac+ed adDacent to one another.
#. crosslin+ing "yrimidines on o""osing strands that are ase "aired to one another.
&. accelerating the "roduction of aasic sites.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) ds #0! rea+s are rare (ith LM light
*eedac+ $) /0! molecules are tem"orary co"ies of information and tend to e aundant. so /0!
damage is not considered to e a serious "rolem
*eedac+ %) Yes. the most aundant class is T5T lin+ages or thymine dimers
*eedac+ #) #ue to geometrical constraints. this is less li+ely than same strand dimeri1ation.
*eedac+ &) Possile. ut rare com"ared to %
143. #uring agarose gel electro"horesis. #0! molecules
!. all migrate at the same rate ecause they have the same charge to mass ratio.
$. migrate according to si1e ecause they all have the same charge to mass ratio.
%. migrate differently de"ending on nucleotide sequence ecause the different ases change the numer
of charges found in a sequence.
#. migrate at rates inde"endent of their sha"e.
&. fail to migrate into the gel at all if they are larger than aout 35.@@@ ase "airs.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) The regular re"eating structure of #0! leads to a uniform charge to mass ratio. ut the total
mass is not the same
*eedac+ $) The regular re"eating structure of #0! leads to a uniform charge to mass ratio. ut the total
mass is not the same. leading to the asis for se"aration
*eedac+ %) The regular re"eating structure of #0! leads to a uniform charge to mass ratio. ut the total
mass is not the same
*eedac+ #) T(o molecules of the same si1e ut different sha"e (ill migrate differently in an agarose gelH
see the 35# gel method for an exam"le.
*eedac+ &) They fail to se"arate (ell due to Fsna+ingG. ut they enter the gel.
148. &. coli #0! is not degraded y its o(n restriction en1ymes ecause
!. the restriction en1ymes are not located in the &. coli nucleus.
$. there are not enough restriction en1yme molecules in the cell.
%. #0! methylases have modified the restriction sites.
#. the en1ymes are made as inactive "recursors efore they are secreted.
&. the &. coli genome does not contain #0! sequences (hich are recogni1ed y its o(n restriction5
modification system.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) $acteria have no nuclei. and restriction en1ymes are active throughout the cell
*eedac+ $) /estriction en1ymes are aundant. ut are "aired (ith modification en1ymesH see %
*eedac+ %) yes. restriction en1ymes are al(ays "aired (ith a modification en1yme (ith the same
recognition site.
*eedac+ #) They are neither made as inactive "recursors. nor are they secretedH they function
intracellularly. see %.
*eedac+ &) 'ee %. &co/I recogni1es a 6 " site. (hich occurs over 1@@@ times in the &. coli genome.
144. 9hich of the follo(ing are exam"les of secondary structure; 1. the sequence of amino acids in a
"rotein 3. the al"ha5helix of myogloin 8. the folding of al"ha5helix onto eta5sheet of triose "hos"hate
isomerase 4. the eta5sheet of an immunogloulin 5. the suunit nature of hemogloin 6. the un5ordered
"ortions of follitro"in =. the eta5turn in any "oly"e"tide
!. all of these
$. only the even5numered items
%. only the odd5numered items
#. 3. 4 and =
&. 3. 4. 6. and =
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #) 15"rimary. 85tertiary. 55quaternary. 65"rimary or secondary.
*eedac+ &) !lso scored as correct -along (ith #2
145. %ytochrome a. a8 -cytochrome oxidase2
!. contains co""er (hich is required for the reduction of oxygen.
$. is a terminal electron acce"tor (hich forms hydrogen "eroxide u"on reduciton of oxygen.
%. can e reduced directly y cytochrome .
#. is not inhiited y caron monoxide.
&. is inhiited directly y rotenone and amytal.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $) :3 is the terminal electron acce"tor and most often forms ,3:.
*eedac+ %) %ytochrome c carries electrons from cytochrome -"art of cytochrome reductase2 to
cytochrome aJa8 -"art of cytochrome oxidase2.
*eedac+ #) Is inhiited y caron monoxide. cyanide. and a1ide.
*eedac+ &) These drugs loc+ electron transfer at 0!#, T reductase.
146. 9hich statement aout glucose metaolism is false;
!. Phos"hofructo+inase is a +ey en1yme (hich can e regulated to control the metaolism of glucose.
$. The "entose "hos"hate "ath(ay must e o"erative in cells (hich synthesi1e significant amounts of
fatty acids.
%. ! five5caron com"ound required for the iosynthesis of /0! can e formed y the oxidation of
glucose.
#. In the cyto"lasm. glucose can e metaoli1ed to "yruvate.
&. Glucose derived from glycogen in muscle serves as a source of lood glucose during fasting.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) P*751 cataly1es the committed ste" of glycolysis.
*eedac+ $) ,4P "ath(ay "rovides the 0!#P, needed for fattty acid synthesis and riose555"hos"hate
for nucleotide synthesis.
*eedac+ %) The ,4P "ath(ay "roduces riose555"hos"hate.
*eedac+ #) Glycolysis ta+es "lace in the cyto"lasm.
*eedac+ &) This is falseH muscle lac+s glucose565"hos"hatase.
14=. The sustrate normally utili1ed as the maDor source of energy y the rain is
!. triglycerides.
$. fatty acids.
%. +etone odies.
#. amino acids.
&. glucose.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $) *atty acid degredation does not ta+e "lace in the rain.
*eedac+ %) 'ome of the rainIs de"endence on glucose shifts to +etone odies during starvation. ut
some glucose is al(ays required.
*eedac+ #)
*eedac+ &) The rain normally accounts for 6@K of the glucose used y the ody. The rain has an
asolute requirement for some glucose even during starvation.
14>. %onsider a single5stranded #0! fragment 1@@@ " long in a solution hyridi1ation ex"eriment. 9hich
of the follo(ing "arameters has the largest effect on the rate of reannealing of this fragment (ith its
com"lementary sequence;
!. The s"ecies from (hich the #0! (as derived
$. The concentration of the com"lementary strand in the solution
%. The fraction of Gs and %s in the sequence of the strand
#. The amount of helicase added to the solution
&. The concentration of detergent in the solution
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) The /!T& of reannealing is strictly determined y the "roaility of collisions et(een
com"lementary strands. and therefore y the concentration of com"lementary strands. This is affected y
the s"ecies. ut is not diagnostic -(hile the concentration is2. *or exam"le. t(o different s"ecies of
acteria (ill give similar reannealing rates ecause their genomes are similarly com"lex.
*eedac+ $) The /!T& of reannealing is strictly determined y the "roaility of collisions et(een
com"lementary strands. and therefore y the concentration of com"lementary strands. The concentration
of com"lementary strands is determined y the com"lexity of the genome of the organism the #0! (as
extracted from.
*eedac+ %) The G<% content strongly affects the staility of du"lex #0!. ut not the /!T& of
reannealing.
*eedac+ #) ,elicases are not added to reannealing ex"eriments. and if they (ere (ould "romote
denaturation of all doule5stranded #0!s
*eedac+ &) The staility of #0! du"lexes is not strongly affected y detergents.
14A. 9hich is 0:T true of the side chain of cysteine;
!. forms disulfide onds
$. "7a is near >
%. is "ositively charged at "hysiological ",
#. is hydro"hilic
&. has a non5asymmetric eta caron
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) *alse. %ysteine has no net charge close to ",P=. ut the side chain can lose a "roton at
al+aline ",.
*eedac+ #) %ysteine is "olar li+e (ater so it is relatively hydro"hilic. ut highly hydro"hoic (hen
cystine-forming a disulfide ond2.
*eedac+ &) The eta caron is not asymmetric ecause of its t(o ound hydrogens.
15@. 9hich "rimers (ill lead to am"lification of 4Y *!M:/IT& G&0& in a P%/ if one strand of the du"lex
tem"late has the follo(ing sequence; 5Q5GGT!%%G!T%54Y *!M:/IT& G&0&5G%!TG!G!T%58Q
!. 5Q5GGT!%%G!T% and 5Q5G%!TG!G!T%
$. 5Q5GGT!%%G!T% and 5Q5G!T%T%!TG%
%. 55G%!TG!G!T% and 5Q5%GT!%T%T!G
#. 5Q5G!T%GGT!%%5and 5Q5%T!G!GT!%G
&. 0one of these "rimer "airs (ill am"lify 4Y *!M:/IT& G&0&
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) first "rimer is right. second "rimer "oints a(ay from target -anneals to the same strand as
the first "rimer2
*eedac+ $)
*eedac+ %) 0o. these oth anneal to the right flan+ of the target -and to each other2
*eedac+ #) 0o. the first "rimer "oints a(ay from the target -anneals to the left flan+2. and the second is
nonsense) it is the reverse of the second site. ut not its com"lement.
*eedac+ &) 0o. see $
151. 9hich is 0:T true aout "rotein folding;
!. disulfide ond formation staili1es a folded structure
$. coo"erative hydrogen ond formation is a driving force
%. "rotein folding is driven in large "art y solvent entro"y
#. hydrogen onding of "rotein side chains to (ater drives "rotein folding
&. van der 9aals forces staili1e the folded state
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %) ,ydro"hoic residues disru"t hydrogen onding et(een (ater molecules. &nergetically it is
more favorale for the hydro"hoic grou"s to e folded to the inside of the "rotein.
*eedac+ #) ,ydro"hoic interaction (ith (ater is the maDor driving force for folding. 'ee %.
*eedac+ &)
153. The sequence of the com"lementary #0! strand for #0! (ith the sequence 5Q5!T%GT!%%GTT! 8 is)
!. 5Q5T!G%!TGG%!!T58Q
$. 5Q5!T%GT!%%GTT!58Q
%. 5Q5T!!%GGT!%G!T58Q
#. 5Q5 !TTG%%!TG%T!58Q
&. 0one of the aove
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) This is com"lementary. ut not anti"arallel.
*eedac+ $) 0o. this is the same. not the anti"arallel com"lement
*eedac+ #) This is reverse -anti"arallel2 ut not com"lementary
*eedac+ &) 0o. see %
158. #eamination of 55methylcytosine in #0!
!. #oes not alter ase "airing and so has no effect on the information encoded
$. %reates uracil in the #0! (hich must e removed y uracil505glycosylase
%. %an e re"aired y dihydrofolate reductase -#,*/2
#. Beads "nici"ally to frameshift mutations
&. *orms thymine (hich leads to mismatches
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) 0o. this changes the ase5"airing s"ecificity -"aired (ith G. no( "airs (ith !2
*eedac+ $) 0o. deamination of % creates L. ut 55methyl L is T.
*eedac+ %) 0o. #,*/ is a en1yme needed during synthesis of nucleotides.
*eedac+ #) 0o. this creates mismatches that lead "rinci"ally to missense mutations
154. Glycine is conserved in nature for the follo(ing reason
!. lac+ of side chain for steric "ac+ing
$. the f dihedral angle confined to 56@
%. hydrogen inding "otential of the / P , side chain
#. often found at "ositions (here no side chain is "ermitted
&. limiting amount of glycyl5t/0!s
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) 'ee #
*eedac+ $)
*eedac+ %)
*eedac+ #) This includes "ac+ing and turns.
*eedac+ &)
155. 9hich of the follo(ing is 0:T true regarding rionucleotide reductase;
!. /0/ converts r0#Ps to d0#Ps y reducing the 3Q caron from 5%,:,5 to 5 %, 3
$. /0/ is suDect to a com"licated system of regulation in (hich the "roduct d0TPs alter its sustrate
s"ecificity.
%. /0/ can e inhiited y the free radical scavenger hydroxyurea.
#. /0/Qs reaction mechanism ma+es use of a stale free radical of a tyrosine generated y an iron atom.
&. /0/ requires regeneration after each catalytic event through a cycle cataly1ed y dihydrofolate
reductase.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) This is true
*eedac+ $) This is true
*eedac+ #) This is true
*eedac+ &) 0o. /0/ does not use a folate derivative to maintain its oxidation state. so #,*/ is not
involved.
156. 9hich modification reaction does not occur at a "oly"e"tide chain terminus;
!. 4yristylation
$. !#P5riosylation
%. !cetylation
#. Glycosyl"hos"hatidylinositol addition
&. amidation
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) !mino terminus
*eedac+ $) !ttachment to a side5chain
*eedac+ %) !mino terminus
*eedac+ #) %aroxyl terminus
*eedac+ &) %aroxyl terminus
15=. !cylovir is an analog of guanosine in (hich the riose ring is disru"ted. 9hich of the follo(ing
reasons ex"lains (hy this drug is useful for treating her"esvirus infections;
!. 0ormal cells are not "ermeale to the drug. ut infected cells are.
$. %ellular #0! "olymerase reDects this sustrate. ut the viral "olymerase uses it.
%. /ionucleotide reductase acts on acyclovir to form a suicide inhiitor that only affects the viral #0!
"olymerase.
#. :nly the viral version of thymidine +inase (ill act on acyclovir. so only infected cells convert it to an
active form.
&. Miral re"lication is faster than cellular re"lication. so the virus is more sensitive to any change in the
level of d0TPs.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) $oth +inds of cell are "ermeale to this drug.
*eedac+ $) The "olymerase doesnIt use acyclovir ecause it is not a tri"hos"hate. not ecause it is
reDected.
*eedac+ %) /0/ does not act on acyclovirH it does not have a sugar moiety so it cannot have a 3I
hydroxyl.
*eedac+ #)
*eedac+ &) 0o. this is Dust confusing.
15>. 9hich is 0:T true aout the structure of an al"ha helix;
!. !mide hydrogen of every "e"tide ond is hydrogen onded
$. 'ide chain alternate et(een a surface location and uried (ithin the helix
%. The rise "er residue in the helix is 1.5 angstroms.
#. Prolines tend to e excluded from helices
&. There are 18 atoms in a hydrogen onded loo"
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) !ll amide hydrogens and caronyl oxygens are hydrogen onded.
*eedac+ $) 'ide5chains are staggered on the surface. There are no interior side5chains.
*eedac+ %)
*eedac+ #) Proline is rigid. (hich reduces structural flexiility. and it has no amide hydrogen for
hydrogen onding.
*eedac+ &)
15A. ! child is found to have a disorder indicating a mutation in a lood clotting factor gene. 9hen the
relevant gene from the child is com"ared to the same sequence from the "arents. an insertion of 8@@ " is
found in one co"y from the child that is not "resent in either co"y from either "arent. 9hich is the li+eliest
ex"lanation;
!. The child can not e the "rogeny of oth of the su""osed "arents since he or she has a different
configuration of genes from the "arents.
$. The child has "roaly suffered a translocation et(een t(o chromosomes
%. This is the result of the trans"osition of a 'I0&
#. This is the result of the trans"osition of a BI0&
&. This is the result of the movement of an intron
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) This (ould e the first thing to chec+. ut the conclusion is not (arrantedH see %
*eedac+ $) ! translocation (ould not cause the oserved change.
*eedac+ %) Yes. 'I0&s are aout 8@@ " long and are trans"osons ca"ale of relocating.
*eedac+ #) BI0&s are ty"ically larger than this. usually aout 6 +".
*eedac+ &) Introns rarely move since fe( are trans"osons. so % is more li+ely.
16@. Poly"e"tides that traverse "hos"holi"id ilayers are often helical for (hich reason;
!. ,elix formation minimi1es solvent contact
$. ,elices have all amides and caronyl grou"s hydrogen onded
%. ,elices have side chains "ac+ed against one another
#. ,elix formation is the one conformation that minimi1es the numer of residues eing in contact (ith
the hydro"hoic ilayer.
&. $eta strands are rare in nature
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) 'ee #
*eedac+ $) Thus they are more li"id solule.
*eedac+ %) 0o. side5chains are staggered to reduce steric hindrance.
*eedac+ #) 0o. all side5chains are on the surface.
*eedac+ &) They are common.
161. 9hich secondary structural element is not ex"osed at the surface of a gloular "rotein;
!. al"ha helix
$. Parallel eta conformers
%. !nti"arallel eta confomers
#. Ty"e I tight turn
&. 8J1@ helix
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) !l"ha helices often have hydro"hoic and hydro"hilic sides.
*eedac+ $) $oth sides of "arallel eta sheets are hydro"hoic. and thus interior structures.
*eedac+ %) !nti"arallel eta sheets have a hydro"hoic and hydro"hilic sides.
*eedac+ #) :ccur at the surface.
*eedac+ &)
163. 9hich of the statements is %://&%T regarding the com"osition of %:/& nucleosome "articles;
!. They contain 5 different +inds of histones
$. They com"act the length of the #0! 3@58@ fold
%. They contain 3 molecules each of ,3!. ,3$. ,8. and ,4
#. They contain aout 4@@ " of #0!
&. They (ra" #0! around themselves aout 8 times
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) %ore histones contain only ,3!. ,3$. ,8. and ,4.
*eedac+ $) 0ucleosomes com"act the #0! 55= fold.
*eedac+ %)
*eedac+ #) ! core nucleosome has aout 146 " of #0! and a @56@ " lin+er.
*eedac+ &) The #0! (ra"s Dust less than t(ice around the nucleosome.
168. 'il+ fiers formed y the sil+ (orm exhiit the follo(ing features. 1. adDacent chains are hydrogen
onded 3. the fier chains are largely extended 8. the sil+ "rotein sho(s a re"eating motif of -'er5Gly5
!la5Gly2 9hich of the follo(ing secondary structural element is li+ely to e he maDor ty"e of element;
!. al"ha helix
$. eta conformers
%. reverse turns
#. omega loo"s
&. 8J1@ helix
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) al"ha helices hydrogen ond (ithin the helix. not et(een chains.
*eedac+ $) The re"eating motif rich in glycine is similar to a collagen tri"le helix. ut that is not a choice.
,ydrogen onding et(een chains suggests a eta conformer.
*eedac+ %)
*eedac+ #)
*eedac+ &)
164. In human somatic tissues. telomeres
!. Get longer (ith age. so inhiiting telomerase (ill ma+e cells younger.
$. Get shorter (ith age. so activating telomerase (ill ma+e cells younger.
%. 4ust e elongated to allo( immortali1ation. so inhiiting telomerase (ill "revent tumors.
#. 4ust e removed to allo( immortali1ation. so inhiting telomerase (ill "revent tumors.
&. 4ust e elongated to allo( immortali1ation. so activating telomerase (ill "revent tumors.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) They get shorter. and telomerase is not causally related to age.
*eedac+ $) Telomerase lengthens telomeres. ut this does not mean the cells get younger.
*eedac+ %) F9illG is "roaly too strong. (e are still in the FmightG stage.
*eedac+ #) Immortali1ation requires a (ay to maintain telomeres. not to remove them.
*eedac+ &) !ctivating telomerase (ould cause lengthening of telomeres. (hich (ould aid tumor gro(th.
165. 9hich is true aout the structure of collagen;
!. !mideJcaronyl hydrogen onding occurs et(een adDacent tro"ocollagen units
$. Gly residues are located in the interior the helix
%. ,ydroxy"roline residues are necessary for crosslin+ing of adDacent helices
#. The rise "er residue of the collagen helix is smaller than that of the a helix
&. #esmosine crosslin+s staili1e firils
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) ! ridge involving one hydroxy"yridinium and t(o hydroxylysines froms et(een
tro"ocollagen molecules.
*eedac+ $) &very 8rd residue faces the cro(ded interior and only glycine (ill fit.
*eedac+ %) 'ee !
*eedac+ #) al"ha helix rise "er residue P 1.5 %ollagen helix P 3.A angstroms
*eedac+ &) #esmosine crosslin+s are found in elastin. not collagen.
166. In error5"rone -':'2 re"air in acteria.
!. /ec! inds to single stranded #0!
$. /ec! assists in the "roteolysis of lex!
%. /ec! acts to assist single stranded #0! search for homologous sequences
#. Transcri"ts encoding en1ymes required for re"air are induced
&. !ll of the aove are correct
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) True. ut so are the other choices. so & is correct.
*eedac+ $) True. ut so are the other choices. so & is correct.
*eedac+ %) True. ut so are the other choices. so & is correct.
*eedac+ #) True. ut so are the other choices. so & is correct.
*eedac+ &) True. ut so are the other choices. so & is correct.
16=. 9hat ty"e of crosslin+ does 0:T staili1e "rocollagen helices;
!. Bysinonorleucine
$. #isulfide ridges
%. ,ydroxy"ridinium structure
#. #esmosine
&. ,ydrogen onding of certain side chains
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #) *ound in elastin.
*eedac+ &)
16>. 9hich statement is 0:T T/L& regarding cell cycle chec+"oints;
!. %hec+"oint "roteins "artici"ate catalytically in the re"air of #0! damage
$. %hec+"oints can e su""ressed y chemicals li+e caffeine. allo(ing ina""ro"riate "assage through the
cell cycle.
%. %hec+"oints delay "rogression of the cell cycle to allo( time for re"airs to occur
#. Boss of chec+"oints leads to genomic instaility
&. %hec+"oints can distinguish accidental doule5strand #0! rea+s from telomeres
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) %hec+"oints are defined to e agents that only !BB:9 re"air y delaying the cell cycle. they
do not "artici"ate in the re"air.
*eedac+ $) This is true
*eedac+ #) This is true. ina""ro"riate "assage through the cycle often leads to loss of chromosomes or
rearrangement.
*eedac+ &) Yes they can. ds rea+s trigger chec+"oints ut telomeres do not.
16A. 9hich is true aout the coo"erative oxygen inding y hemogloin;
!. :xygenated hemogloin has the heme iron atom "ushed out of the "lane of the heme.
$. :xygen inding induces a series of salt lin+s formed et(een the four chains.
%. :xygenation induces movement of the t(o al"haJeta suunit "airs.
#. :xygen inding alters the numer of contacts et(een the t(o al"ha suunits.
&. :yxgenation of the 4 suunits occurs in an "recise order
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) *alse. In deoxyhemogloin the iron is "ulled out of the "lane y a histidine. $inding of
oxygen counteracts the histidineIs "ull.
*eedac+ $) *alse. oxygen inding requires that salt lin+s e ro+en.
*eedac+ %) .
*eedac+ #) There is al(ays little contact et(een the t(o al"ha suunits or the t(o eta suunits
*eedac+ &) 0o. inding of :3 to one heme affects the affinity of the other hemes. ut there is no "recise
order of oxygenation.
1=@. 'equencing #0! molecules y dideoxy nucleoside tri"hos"hate termination requires
!. a mixture of normal d0TPs and modified forms (ith a 3Qtri"hos"hate
$. a mixture of normal d0TPs and modified forms (ith a 8Qtri"hos"hate
%. a mixture of normal d0TPs and modified forms lac+ing the 3Qhydroxyl
#. a mixture of normal d0TPs and modified forms lac+ing the 8Qhydroxyl
&. a mixture of normal d0TPs and modified forms lac+ing the 5Qhydroxyl
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) d0TPs have no 3I hydroxyl
*eedac+ $) terminators have no 8I hydroxyl
*eedac+ %) normal d0TPs already lac+ the 3I hydroxyl
*eedac+ #) Yes. the 8I hydroxyl is the nucleo"hile required for "olymeri1ation. so loss of the grou"
creates a chain terminator.
*eedac+ &) Polymeri1ation requires a 5I tri"hos"hate. so a form lac+ing this (ould never e incor"orated
and could not act as a terminator.
1=1. ! "hysician told a "atient that she had no $ohr effect. 9hat amino acids (ere missing in her
hemogloin;
!. caroxyl5terminal residues
$. heme inding ligands
%. "roximal *> ,is
#. $> Glu
&. eta chain #PG inding residues
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) ,< is ound to caroxy terminal ,is146 of the eta chain and to terminal al"ha amino
grou"s. %:3 inds to the terminal al"ha amino grou"s.
*eedac+ $)
*eedac+ %) This ,is "ulls the iron out of the "or"hyrin "lane in deoxyhemogloinH it is not associated
(ith the $ohr effect.
*eedac+ #)
*eedac+ &)
1=3. &. coli #0! is not degraded y its o(n restriction en1ymes ecause
!. the restriction en1ymes are activated only outside the nucleus.
$. the restriction en1ymes are trans"orted out of the nucleus.
%. #0! methylases modify the restriction sites.
#. the restriction en1ymes are activated only after they are secreted out of the cell.
&. The &. coli genome does not contain #0! sequences (hich are recogni1ed y its o(n restriction5
modification system.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) $acteria have no nuclei. and restriction en1ymes are active throughout the cell
*eedac+ $) $acteria have no nuclei. and restriction en1ymes are active throughout the cell
*eedac+ %) yes. restriction en1ymes are al(ays "aired (ith a modification en1yme (ith the same
recognition site.
*eedac+ #) /estriction en1ymes act inside the cell.
*eedac+ &) 'ee %. &co/I recogni1es a 6 " site. (hich occurs over 1@@@ times in the &. coli genome.
1=8. ! "atient had troule (ith exercise and you as the "hysician found only eta chains in his
hemogloin. ,is lood (as right red on the arterial side and (asnQt the usual lue on the venous side. It
(as redU 9hy (as the hemogloin reluctant to give u" enough oxygen in the tissues for the man to
exercise comfortaly;
!. #eficiency of 3.85#PG
$. :verex"ression of fetal hemogloin chains
%. !normally high oxygen inding affinity and no coo"erativity
#. ,emogloin mutation "revented inding of %:3
&. Tissues (ere lac+ing in myogloin
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) This (ould cause hemogloin to have a higher oxygen affinity. ut this "atient has a stated
anormality of only eta chains.
*eedac+ $)
*eedac+ %) This could e ,, disease. !ccumulation of eta tetramers (hich have no heme5heme
interactions.
*eedac+ #) $inding of %:3 normally lo(ers hemologinIs affinity for @3. so loss of %@3 inding (ould
increase oxygen affinity. ut the stated anormality is missing al"ha chains.
*eedac+ &) In a study of mice (ho lac+ed myogloin no significant effects (ere found.
1=4. Gout can e caused y all of the follo(ing &?%&PT
!. Inhiition of rionucleotide reductase
$. underexcretion of uric acid
%. dietary and environmental factors
#. errors in the feedac+ regulation of "urine iosynthesis
&. over"roduction of uric acid
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) This affects only #0! re"lication. not "urine turnover.
*eedac+ $) This causes elevated uric acid levels. leading to gout
*eedac+ %) These can cause increased uric acid y altering the rate of synthesis or the rate of excretion
*eedac+ #) &xcess "urine synthesis causes excess turnover. leading to high urate and gout.
*eedac+ &) &xcess uric acid is the cause of gout.
1=5. :ne of your "atients (as a mechanic (ho (or+ed on automoile exhaust systems exclusively. ,e
came in to the clinic dro(sy and (ith "in+ chee+s. ,e claimed he often fainted (hen he exerted himself.
9hat did his hemogloin analysis sho(;
!. Bo( oxygen inding due to high levels of caroxyhemogloin -, %:2
$. !normally lo( levels of eta chains
%. !normally lo( levels of gamma chains
#. 'ustitution of *> ,is y Tyr
&. 4onomeric hemogloin molelcules
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) %: inds tightly to one heme shifting hemogloin to the relaxed. high :3 affinity. state. Thus
the affected , is unale to release :3 to the tissues.
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
1=6. Identify the main ty"e of mutation caused y ty"e II to"oisomerase inhiitors.
!. $ase "air sustitutions
$. *rameshift mutations
%. #eletions
#. Insertions
&. Translocations
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) *ailure of ty"e II to"o causes ds #0! rea+s. leading to translocations
*eedac+ $) *ailure of ty"e II to"o causes ds #0! rea+s. leading to translocations
*eedac+ %) *ailure of ty"e II to"o causes ds #0! rea+s. leading to translocations
*eedac+ #) *ailure of ty"e II to"o causes ds #0! rea+s. leading to translocations
*eedac+ &) *ailure of ty"e II to"o causes ds #0! rea+s. leading to translocations
1==. ! "atient had chains that (ere colorless. 9hich "art of the hemogloin molecule may e defective;
!. al"ha5terminal residues
$. heme inding residues
%. #PG inding residues
#. the "roximal *> ,is
&. ilireuin inding site
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $) It is the heme that gives oxegenated lood its red color.
*eedac+ %)
*eedac+ #)
*eedac+ &)
1=>. ! mutated virus is found to co"y its genome faster than it used to. It is very li+ely that at the same
time it also acquired
!. ! much smaller genome
$. ! much larger genome
%. ! lo(er error frequency
#. ! higher error frequency
&. ! narro(er host s"ecificity
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) This is unli+ely since it (ould "roaly inca"acitate the virus com"letely
*eedac+ $) This (ould not cause faster re"lication
*eedac+ %) *aster co"ying is associated (ith higher error rates.
*eedac+ #) Yes. s"eed and accuracy are a tradeoff
*eedac+ &) This (ould not e lin+ed to re"lication rate in any ovious straightfor(ard (ay.
1=A. ! (itch doctor (ith sic+le cell anemia claims his disease im"roved (hen he dran+ his o(n urine.
9hat "ossile enefit may e occurring (ith sic+le cell hemogloin;
!. Protease in urine degraded aggregated , ' therey restoring normal cell sha"e
$. Bo( ", of urine soluili1ed aggregated , ' (ith restoration of normal cell sha"e
%. %yanate formed from urea loc+ed the al"ha amino residues "recluding salt ridges
#. Lrea in urine soluili1ed aggregated , '
&. ,e otained extra iron atoms for ne( hemogloin synthesis
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) %yanate caramoylates the terminal amino grou"s ehaving as a reactive analog of %:3.
*eedac+ #)
*eedac+ &)
1>@. 9hich of the follo(ing statements is 0:T reasonale. ,emogloin (ould not e an effective oxygen
carrier if it (ere a "lasma "rotein rather than "resent (ithin erythrocytes. ecause ... ;
!. suunits may dissociate and e filtered in the +idney.
$. there is no #PG in serum.
%. the %:3 trans"orted y hemogloin requires an en1yme (ithin the erythrocyte.
#. there is no (ay to maintain the heme iron in the ferrous state.
&. more difficult to maintain "ro"er ratios of #PG and hemogloin concentrations
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) True. large erythrocytes esca"e filtering.
*eedac+ $) :3 affinity of , (ithin erythrocytes is lo(er than , in "lasma ecause in erythrocytes #PG
is maintained at a""roximately the same molar concentration as ,.
*eedac+ %) True. most %:3 is trans"orted as icaronate. (hich is fromed in erythrocytes y caronic
anhydrase.
*eedac+ #) $e(are of lan+et statements. There is "roaly a (ay.
*eedac+ &) 'ee $.
1>1. 9hat is needed to achieve Mmax in an en1yme reaction;
!. en1yme concentration aove the 7m
$. "hysiological ",
%. a 1)1 ratio of en1yme and sustrate
#. great luc+
&. excess sustrate
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) 7m is the concentration of sustrate needed to achieve 1J3 maximal velocity.
*eedac+ $)
*eedac+ %) ! 1)1 ratio is not suffient ecause sustrate (ould e converted to "roduct. and then active
sites (ould e unoccu"ied. There must e more sustrate to +ee" the en1yme saturated.
*eedac+ #)
*eedac+ &) Mmax is achieved (hen all of the active sites are occu"ied y sustrate. 'ee %.
1>3. 'u""ose the ,is in the charge transfer net(or+ of chymotry"sin (as mutated to !la. 9hat effect
(ould that have on catalysis;
!. all en1yme molecules (ould end u" in a stale. acylated intermediate.
$. "e"tide sustrates (ould not ind
%. no formation of acylated intermediate
#. no change in activity
&. en1yme (ould not fold
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) 'ee %.
*eedac+ $)
*eedac+ %) The alanine (ould not ta+e ,< from serine as histidine does. Thus the serine (ould not e
ale to attac+ and form the acylated intermediate.
*eedac+ #) !ctivity (ould change dramatically.
*eedac+ &) The folding my differ some from normal chymotry"sin. ut the "rotein (ould still fold.
1>8. Increasing the concentration of d!TP directly causes rionucleotide reductase to
!. Increase the rate of "roduction of d%#P
$. Increase the rate of "roduction of dG#P
%. #ecrease the rate of "roduction of r%#P
#. #ecrease the rate of "roduction of dL#P
&. Increase the rate of "roduction of dTTP
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) Increased d!TP decreases the activity of /0/ for all sustrates and "roducts
*eedac+ $) Increased d!TP decreases the activity of /0/ for all sustrates and "roducts
*eedac+ %) Increased d!TP decreases the activity of /0/ for all sustrates and "roductsH ut r%#P is not
a "roduct of /0/.
*eedac+ #) Increased d!TP decreases the activity of /0/ for all sustrates and "roducts
*eedac+ &) Increased d!TP decreases the activity of /0/ for all sustrates and "roducts
1>4. 9hich of the follo(ing conditions (ould "romote denaturation of doule5stranded #0!;
!. #ecreasing the tem"erature
$. !dding 0a%l
%. !dding detergent
#. Increasing the ", -aove neutral2
&. #ecreasing the concentration of organic solvent -formamide. for exam"le2
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) #0! denatures at high tem"eratures so this (ould "romote the native form
*eedac+ $) 0a%l contriutes to charge shielding for the "hos"hodiester ac+one. staili1ing the du"lex
*eedac+ %) #etergents donIt a""recialy alter the staility of #0! du"lexes
*eedac+ #) Increased ", destaili1es ase "airing interactions and therefore "romotes denaturation
*eedac+ &) Increasing organic solvents decreases the staility of #0! du"lexes due to the decrease in
energy derived from ase stac+ing. so decreasing the concentration (ould "romote staili1ation
1>5. $acterial "lasmids
!. are usually linear #0! molecules.
$. can confer resistance to many antiiotics simultaneously.
%. cannot e transferred from one cell to another.
#. are a disadvantage to their hosts.
&. are not found in human "athogens.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) Plasmids are ty"ically circular
*eedac+ $) 'cary. and true
*eedac+ %) 4any "lasmids encode machinery for transferring themselves to other cells
*eedac+ #) 4any "lasmids confer resistance to antiiotics (hich "rovides a strong advantage to the host
if that sustance is encountered.
*eedac+ &) Lnfortunately. this is not true.
1>6. 55"hos"horiosyl515"yro"hos"hate -P/PP2 is an intermediate in
!. the de novo synthesis of "urine nucleotides
$. the de novo synthesis of "yrimidine nucleotides
%. the salvage "ath(ay for the synthesis of "urine nucleotides
#. ! and %
&. !. $ and %
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) Yes. it is activated as the committed ste" for "urine synthesis. ut $ and % are also true so
the ans(er is &.
*eedac+ $) Yes. it is used to FscavengeG the "reformed ase orotate. ut ! and % are also true. so the
ans(er is &.
*eedac+ %) Yes. it is comined (ith hy"oxanthine or guanine y ,GP/Tase. ut ! and $ are also true so
the ans(er is &
*eedac+ #) Yes. ut $ is also true. so the ans(er is &
*eedac+ &)
1>=. :ne of the strands of a doule5stranded. 1@ +" #0! du"lex has the follo(ing numers of ase
residues) adenine -!2 5 38@@. thymine -T2 5 3>@@. The ase com"osition of the (hole doule5stranded
molecule (ill e
!. a 5 51@@. t 5 51@@. g 5 4A@@. c 5 4A@@
$. a 5 46@@. t 5 54@@. g 5 56@@. c 5 44@@
%. a 5 56@@. t 5 56@@. g 5 44@@. c 5 44@@
#. a 5 46@@. t 5 56@@ . g 5 54@@. c 5 44@@
&. There is not enough information to determine the overall ase com"osition
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) #ue to "airing rules. the other strand has 38@@ T and 3>@@ !. for a total of 51@@ ! and 51@@
T. The remainder must e equal numers of G and % for the same reason. ma+ing 4A@@ of each.
*eedac+ $) #ue to "airing rules. the other strand has 38@@ T and 3>@@ !. for a total of 51@@ ! and 51@@
*eedac+ %) #ue to "airing rules. the other strand has 38@@ T and 3>@@ !. for a total of 51@@ ! and 51@@
*eedac+ #) #ue to "airing rules. the other strand has 38@@ T and 3>@@ !. for a total of 51@@ ! and 51@@
*eedac+ &) #ue to "airing rules. the other strand has 38@@ T and 3>@@ !. for a total of 51@@ ! and 51@@
1>>. If you denature similar amounts of the follo(ing 5 #0! sam"les then return them to conditions that
favor renaturation. (hich (ill remain the most single5stranded the longest;
!. ,uman liver nuclear #0!
$. Maccinia -viral2 #0!
%. &. coli #0!
#. Yeast #0!
&. eye of ne(t #0!
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) The rate of reannealing for any "iece of #0! is determined y the concentration of the
com"lementary strand. Given the same amount of total #0!. the sam"le (ith the sim"lest com"osition
-the fe(est different sequences2 (ill have the highest concentration of each sequence and (ill anneal the
fastest. In this case the sim"lest sam"le is the viral #0!.
*eedac+ $) The rate of reannealing for any "iece of #0! is determined y the concentration of the
*eedac+ %) The rate of reannealing for any "iece of #0! is determined y the concentration of the
*eedac+ #) The rate of reannealing for any "iece of #0! is determined y the concentration of the
*eedac+ &) The rate of reannealing for any "iece of #0! is determined y the concentration of the
1>A. The "rocessivity of #0! "olymerases
!. increases in the "resence of ligases
$. decreases in the "resence of helicases
%. decreases in the "resence of single strand inding "roteins
#. increases in the "resence of :+a1a+i factors
&. increases in the "resence of clam" "roteins
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) Bigases seal nic+s after "olymerase is finished. they do not affect "rocessivity
*eedac+ $) ,elicases un(ind the tem"late. ma+ing "rogression easier and therefore increase the
"rocessivity of "olymerases
*eedac+ %) ''$s straighten the tem"late and therefore increase the "rocessivity of "olymerases.
*eedac+ #) There is no such thing
*eedac+ &) %lam" "roteins "revent dissociation of the "olymerase from its tem"late and therefore
increase the "rocessivity
1A@. ! acterial culture gro(n for many generations in a ElightE -1402 medium (as transferred to a
EheavyE -1502 medium. !fter the #0! had een co"ied 8 times under the ne( conditions. (hat (ould e
the relative distriution of #0! containing t(o light strands -BB2. one heavy and one light strand -,B2. and
t(o heavy strands -,,2;
!. 4 ,,)4 ,B)@ BB
$. 6 ,,)1,B)1 BB
%. 4 ,,)3 ,B) 3
BB
#. 6 ,,)3 ,B) @ BB
&. 3 ,,)4 ,B) 3 BB
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) !fter one co"y. the #0! (ould all e ,B. after 3 it (ould e 1 ,B)1 ,,. after 8 it (ould e 1
,B)8 ,,.
*eedac+ $) !fter one co"y. the #0! (ould all e ,B. after 3 it (ould e 1 ,B)1 ,,. after 8 it (ould e 1
,B)8 ,,. There (ould e no BB after the first co"y.
*eedac+ %) !fter one co"y. the #0! (ould all e ,B. after 3 it (ould e 1 ,B)1 ,,. after 8 it (ould e 1
*eedac+ #) !fter one co"y. the #0! (ould all e ,B. after 3 it (ould e 1 ,B)1 ,,. after 8 it (ould e 1
,B)8 ,, -P6 ,,)3 ,B2
*eedac+ &) !fter one co"y. the #0! (ould all e ,B. after 3 it (ould e 1 ,B)1 ,,. after 8 it (ould e 1
1A1. In methylation5directed mismatch re"air in acteria
!. 4ut' inds to mismatches in du"lex #0!
$. The methylated strand is Dudged to e the ne(er strand
%. 4utB inds to methylated #0! strands
#. 4ethylation of cytosine leads to deamination to thymine
&. /ec! ma+es an incision only at hemimethylated sites
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $) 4ethylation indicates that this #0! is old since this modification must have occured efore
#0! re"lication
*eedac+ %) 4ut, recogni1es the methylation status
*eedac+ #) This is true. ut irrelevant to the question as+ed
*eedac+ &) /ec! acts in ':' and in recomination. ut not in mismatch re"air
1A3. 4uscle can carry out all of the follo(ing "rocesses &?%&PT
!. transamination of amino acids.
$. synthesis of glycogen.
%. synthesis of glucose from alanine.
#. oxidation of +etone odies.
&. "hos"horylation of creatine.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) Gluconeogenesis occurs in the liver and +idney.
*eedac+ #)
*eedac+ &)
1A8. Telomeres are different from ro+en ends of #0! ecause
!. They have a series of re"eats of a "articular 651@ ase "air sequence
$. They are staili1ed y the "resence of short /0! "rimers needed to com"lete re"lication
%. They are recogni1ed and extended y telomerase
#. :nly ! and % are correct
&. !. $. and % are all correct
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) This is true. ut so is %
*eedac+ $) This Dust confusing
*eedac+ %) This is true. ut so is !
*eedac+ #)
*eedac+ &) $is incorrect
1A4. 4utations caused y one of the follo(ing agents almost al(ays inactivate genes s"ecifying "rotein
it;
!. LM light
$. cis5"latin
%. intercalating agents
#. EmustardE gases
&. 55romouracil
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) 0o. LM light ty"ically causes single ase changes. (hich are as ad for "roteins as for /0!s
*eedac+ $) 0o. this is ty"ically a crosslin+er leading to doule5strand rea+s.
*eedac+ %) Yes. these cause insertions and deletions leading to frame5shifts that are much (orse for
:/*s than for /0!s
*eedac+ #) 0o. these are ty"ically a crosslin+ers leading to doule5strand rea+s.
*eedac+ &) 0o. this causes an enforced tautomeric shift leading to single ase changes.
1A5. 9hich "rimers (ill lead to am"lification of 4Y *!M:/IT& G&0& in a P%/ if one strand of the du"lex
tem"late has the sequence elo(; 5Q5GGT!%%G!T%54Y *!M:/IT& G&0&5G%!TG!G!T%58Q
!. 5Q5GGT!%%G!T% and 5Q5G%!TG!G!T%
$. 5Q5GGT!%%G!T% and 5Q5G!T%T%!TG%
%. 5Q5G%!TG!G!T% and 5Q5%GT!%T%T!G
#. 5Q5G!T%GGT!%% and 5Q5%T!G!GT!%G
&. 5Q5%%!TGG%T!G and 5Q5G%!TG!G!T%
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) The first "rimer is correct. ut the second one anneals to the same strand and "oints a(ay
from the target
*eedac+ $)
*eedac+ %) The first "rimer "oints a(ay from the target and the second is nonsense -com"lementary ut
not anti"arallel2
*eedac+ #) The first "rimer is correct. ut the second is nonsense -anti"arallel. ut not com"lementary2
*eedac+ &) The first "rimer is com"lementary ut not anti"arallel. and the second "oints a(ay from the
target.
1A6. Pyruvate caroxylase of liver is activated most directly y
!. acetyl %o!.
$. "hos"hoenol"yruvate.
%. a high ratio of !#PJ!TP.
#. calcium ions.
&. cyclic !4P.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) allosteric activation of the 1st ste" of gluconeogenesis.
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
1A=. #0! sequencing de"ends on generating a set of molecules that terminate at every "ossile "osition.
This is done y sto""ing the synthesis
!. using modified nucleotides lac+ing the 8Q hydroxyl grou"
$. using a #0! "olymerase "urified from a thermo"hilic organism
%. using modified nucleotides "hos"horylated at the 5Q hydroxyl
#. using modified nucleotides (ith deaminated ases
&. using a non5"rocessive #0! "olymerase
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) Yes. the 8I hydroxyl is a necessary nucleo"hile for the "olymeri1ation reaction
*eedac+ $) 'ometimes. ut this is not a necessary feature contriuting to chain termination
*eedac+ %) 0ormal nucleotides are "hos"horylated at the 5I "osition
*eedac+ #) The ases contriute to s"ecificity ut do not cause chain termination
*eedac+ &) This (ould not "rovide s"ecific chain termination
1A>. 9hich of the follo(ing is a general feature of oth #0! and /0!;
!. in vivo they are usually doule helical structures formed from t(o se"arate chains.
$. Their "hos"hodiester ac+ones are stale in solutions aove ", 13.
%. They are made "artly of com"lementary G5% ase "airs.
#. They oth have "hos"hodiester onds lin+ing the 5Q and 3Q hydroxyls of the riose grou"s.
&. They interact (ith histones to form nucleosomes.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) /0! is usually single5stranded. so any du"lexes are formed from intra5strand interactions
*eedac+ $) /0! is unstale at high ", due to the nucleo"hilic attac+ y the 3I hydroxyl on the
"hos"hodiester ac+one.
*eedac+ %)
*eedac+ #) This is true of the 5I and 8I grou"s
*eedac+ &) /0! is not found in nucleosomes
1AA. 9hich one of the follo(ing en1ymes might e ex"ected to e more active as a consequence of higher
citrate concentration;
!. "yruvate caroxylase
$. "hos"hofructo+inase
%. citrate synthase
#. acetyl %o! caroxylase
&. "yruvate dehydrogenase
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) 'timulated y acetyl %o!.
*eedac+ $) Inhiited y citrate.
*eedac+ %) 4a+es citrate. inhiited y !TP.
*eedac+ #) %itrate induces "olymeri1ation of the suunits.
*eedac+ &)
3@@. The sequence of the com"lementary #0! strand for #0! (ith the sequence 5Q5!T%GT!%%GTT! 8Q is)
!. 5Q5T!G%!TGG%!!T58Q
$. 5Q5TG!%!G!GT!G!58Q
%. 5Q5T!!%GGT!%G!T58Q
#. 5Q5!TTG%%!TG%T!58Q
&. 5Q5!T%GT!%%GTT!58Q
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) %om"lementary. ut not anti"arallel
*eedac+ $) 0onsense
*eedac+ %) This com"lementary and anti"arallel
*eedac+ #) !nti"arallel. ut not com"lementary
*eedac+ &) 0ot com"lementary or anti"arallelH this is the same as the sequence in the question
3@1. :ut of the storage forms in humans. (hich is largest in terms of calorie yield is
!. "rotein.
$. glucose.
%. glycogen.
#. triglyceride.
&. li"o"rotein.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) 0ot really a storage form. 4 %alJg.
*eedac+ $) 0ot a storage form.
*eedac+ %) ! carohydrate. 4 %alJg.
*eedac+ #) A %alJg.
*eedac+ &) 0ot a storage form.
3@3. The melting tem"erature of doule stranded #0!
!. increases (ith increasing guanine content
$. decreases (ith increasing cytosine content
%. increases (ith decreasing guanine content
#. decreases (ith decreasing adenine content
&. increases (ith increasing thymine content
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) G<% ase "airs are more stale than !<T so as G content rises so does the Tm
*eedac+ $) G<% ase "airs are more stale than !<T so as % content rises so does the Tm
*eedac+ %) G<% ase "airs are more stale than !<T so as G content rises so does the Tm
*eedac+ #) G<% ase "airs are more stale than !<T so as ! content dro"s the Tm rises
*eedac+ &) G<% ase "airs are more stale than !<T so as T content increases the Tm dro"s
3@8. /educing equivalents generated during glycolysis in a normal liver cell
!. enter the mitochondria as "rotons.
$. are used in the "entose "hos"hate "ath(ay.
%. are trans"orted into mitochondria in the form of malate.
#. enter the mitochondria as reduced glutathione.
&. enter the mitochondria as 0!#,.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) 4alate5!s"artate shuttle.
*eedac+ #)
*eedac+ &) The mitochondrial memrane is im"ermeale to 0!#,.
3@4. 9hat structural feature of #0! accounts for its staility to al+aline hydrolysis;
!. The "resence of hydrogen onding et(een "urines and "yrimidines.
$. The lac+ of a 3Q5hydroxyl in the "entose
%. The lac+ of a 8Q5hydroxyl in the "entose
#. The "resence of thymine in #0!.
&. The asence of uracil from #0!.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) The 3I hydroxyl is res"onsile for the instaility of /0!. and its removal is the asis for the
increased staility of #0!
*eedac+ $) The 3I hydroxyl is res"onsile for the instaility of /0!. and its removal is the asis for the
*eedac+ %) The 3I hydroxyl is res"onsile for the instaility of /0!. and its removal is the asis for the
*eedac+ #) The 3I hydroxyl is res"onsile for the instaility of /0!. and its removal is the asis for the
*eedac+ &) The 3I hydroxyl is res"onsile for the instaility of /0!. and its removal is the asis for the
3@5. !ll of the follo(ing can stimulate the activity of muscle glycogen "hos"horylase &?%&PT
!. calcium ions.
$. e"ine"hrine.
%. cyclic !4P.
#. "hos"horylase +inase.
&. glucagon.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &) Glucagon does not affect muscle.
3@6. 9hich of the follo(ing "ro"erties of nucleotides does 0:T affect the structure of nucleic acids;
!. The ases are hydro"hoic
$. The "hos"hates are negatively charged at neutral ",
%. The ases can each form multi"le hydrogen onds
#. The ases asor ultraviolet light at a (avelength near 36@ nm
&. The sugar grou" is highly (ater solule
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) This "rovides the main driving force for formation of the du"lex
*eedac+ $) The re"ulsion of the ac+ones is a significant force affecting the structure and staility of
du"lexes
*eedac+ %) The aility to form hydrogen onds is an im"ortant determinant of the s"ecificity of the
interaction et(een strands -the com"lementarity2.
*eedac+ #) This is true ut does not affect the structure of the du"lex
*eedac+ &) This "rovides soluility to nucleic acids
3@=. !ccelerated de novo "urine iosynthesis in the Besch50yhan syndrome is "roaly due to
!. de"ression of 55"hos"horiosyl515"yro"hos"hate amidotransferase
$. increased availaility of 55"hos"horiosyl515"yro"hos"hate
%. defective feedac+ inhiition of rionucleotide reductase
#. increased uric acid synthesis
&. increased hy"oxanthine5guanine "hos"horiosyltransferase
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) Bac+ of ,GP/Tase causes the level of its sustrate P/PP to increase. leading to higher rates
of activation and "urine synthesis.
*eedac+ $) Bac+ of ,GP/Tase causes the level of its sustrate P/PP to increase. leading to higher rates
*eedac+ %) Bac+ of ,GP/Tase causes the level of its sustrate P/PP to increase. leading to higher rates
*eedac+ #) Bac+ of ,GP/Tase causes the level of its sustrate P/PP to increase. leading to higher rates
*eedac+ &) Bac+ of ,GP/Tase in this syndrome causes the level of its sustrate P/PP to increase. leading
to higher rates of activation and "urine synthesis.
3@>. ! common source of mutations in humans starts (ith the deamination of
!. 55methyl5thymine
$. 55fluoro5uracil
%. 55methyl5cytosine
#. 55methyl5uracil
&. 55methyl5adenine
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) Thymine already has a 55methyl grou"
*eedac+ $) This is not usually found in normal cells
*eedac+ %) Yes. this leads to formation of T. (hich is then a sim"le mismatch (ith the G usually found
o""osite %.
*eedac+ #) This is thymine -(hich is already deaminated2.
*eedac+ &) 0o such thing
3@A. In #0! re"lication in human cells
!. re"lication initiates at aout 4@@@ sites called origins
$. a #0! "olymerase that incor"orates ases in the 8Q to 5Q orientation is found
%. re"lication is continuous on oth strands
#. the re"lication or ' "hase lasts aout > hours
&. re"lication and segregation overla" to allo( shorter division cycles
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) ,umans have aout 4@.@@@ origins of re"lication
*eedac+ $) 0o "olymerase (ith this "olarity is +no(n
*eedac+ %) /e"lication is continuous on the leading strand ut discontinous on the lagging strand
*eedac+ #)
*eedac+ &) This is a tric+ that only "ro+aryotes (ith single re"lication origins "er genome can "ull off
31@. The com"ound (hich acce"ts a t(o5caron fragment from acetyl5%o! to initiate the citric acid cycle
is
!. oxalosuccinate.
$. oxalate.
%. oxaloacetate.
#. oxytocin.
&. oxyutyrate.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) %itrate synthase cataly1es) oxaloacetate < acetyl %o! 5556 %o! < citrate.
*eedac+ #) ! "ituitary hormone.
*eedac+ &)
311. #0! "olymerase. a "rimed #0! tem"late. and the four deoxynucleoside tri"hos"hates -d0TPs2 are
mixed together. 9hich is the most im"ortant in determining the ase com"osition -the numer of !s. Gs.
%s. and Ts2 of the "roduct #0!;
!. the addition of a "rocessivity clam"
$. the ratios of the four d0TPs availale
%. the s"ecies from (hich the tem"late #0! (as "urified
#. the ty"e of "rimer used in the reaction
&. the s"ecies from (hich the #0! "olymerase (as "urified.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) This is im"ortant for the rate of synthesis. ut only the tem"late determines the com"osition
of the "roduct.
*eedac+ $) These are necessary for re"lication. ut only the tem"late determines the com"osition of the
"roduct.
*eedac+ %) The com"osition of the tem"late determines the com"osition of the "roduct. so the source of
the #0! tem"late determines the com"osition.
*eedac+ #) The "rimer allo(s re"lication. ut only the tem"late determines the com"osition of the
"roduct.
*eedac+ &) #0! "olymerase Dust ta+es instructions from the tem"late. it doesnIt matter (here it came
from
313. The increase in lood sugar level resulting from e"ine"hrine inDection can est e ex"lained y (hich
one of the follo(ing;
!. 'ynthesis of carohydrate from fat
$. !sor"tion of carohydrate from the digestive tract
%. Biver glycogenesis
#. Biver glycogenolysis
&. Gluconeogenesis
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %) Phos"horylated glycogen synthase in inactive.
*eedac+ #) Phos"horylated glycogen "hos"horylase is active and glycogen in ro+en do(n "roviding
glucose.
*eedac+ &) 0ot directly affected y e"ine"hrine.
318. 0ucleotide excision re"air is +no(n to need all of the follo(ing en1ymes &?%&PT (hich one;
!. ! nuclease
$. ! ty"e I to"oisomerase
%. ! #0! helicase
#. ! #0! ligase
&. ! #0! "olymerase
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) The excision itself is "erformed y a nuclease
*eedac+ $) 0o role is +no(n at this "oint for a ty"e I to"o in 0&/
*eedac+ %) ! helicase is need to remove the damaged #0! strand after it has een cli""ed y a nuclease
*eedac+ #) ligase is needed to seal the nic+ "roduced y resynthesis of the ga" "roduced y removing
the damaged #0!
*eedac+ &) #0! "olymerase resynthesi1es the #0! to fill the ga" "roduced y removal of the damaged
#0!
314. !llosteric inhiitors of regulatory en1ymes most li+ely influence en1yme activity y
!. inducing a conformational change in the en1yme.
$. "romoting a covalent modification of the en1yme.
%. inding to the active site of the en1yme.
#. reacting (ith the sustrate.
&. "romoting de"hos"horylation of the en1yme.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %) This is com"etative inhiition.
*eedac+ #)
*eedac+ &)
315. Photolyases
!. Lse incident light to rea+ 05glycosidic onds
$. 0ic+ #0! molecules near sites of damage to initiate re"air synthesis
%. 'eal nic+s in the "hos"hodiester ac+one of #0! molecules
#. /everse the formation of cycloutane dimers caused y LM light.
&. %ut #0! at hemi5methylated sites.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) This (ould cause. not re"air. damage
*eedac+ $) Photolyases reverse damage y undoing the formation of cycloutane rings
*eedac+ %) This is the Do of ligase. "hotolyases reverse damage y undoing the formation of
cycloutane rings
*eedac+ #)
*eedac+ &) This is the Do of 4ut,. "hotolyases reverse damage y undoing the formation of cycloutane
rings
316. In the liver. 8Q.5Q5!4P increases the activity of all the follo(ing en1ymes &?%&PT
!. glycogen "hos"horylase.
$. fructose 3.6 is"hos"hatase.
%. "yruvate +inase.
&. cyclic !4P5de"endent "rotein +inase.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) Phos"horylation inactivates "yruvate +inase.
*eedac+ #)
*eedac+ &)
31=. ! #0! molecule is laeled and used to locate com"lementary strands in a restriction en1yme digest
of genomic #0! se"arated y electro"horesis. This is called a
!. 0orthern lot
$. 9estern lot
%. 'outhern lot
#. &astern lot
&. In+ lot
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) 0orthern lots contain immoili1ed /0!. not #0!
*eedac+ $) 9estern lots contain immoili1ed "roteins and are "roed (ith antiodies
*eedac+ %)
*eedac+ #) 0o such thing. for some strange reason
*eedac+ &) :f course not. I (as Dust eing silly
31>. The statements elo( refer to discrete ste"s involved in the rea+do(n of muscle glycogen to
glucose 15"hos"hate. 'elect the a""ro"riate sequence from the list elo(.
1. "hos"horylase 556 "hos"horylase a
3. dissociation of the c!4P de"endent +inase
8. activation of adenylate cyclase
4. "hos"horylation of "hos"horylase +inase
!. 1.3.8.4
$. 3.8.1.4
%. 8.3.4.1
#. 3.8.4.1
&. 8.4.1.3
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
31A. %ells lac+ing "58 are anormal ecause they
!. lac+ en1ymes needed for ase excision re"air
$. fail to enter ' "hase if their #0! is damaged
%. arrest in mitosis in the "resence of high levels of caffeine
#. fail to die after ex"osure to #0! damage
&. ! and % are oth correct
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) 0o. $&/ is normal in "58 mutants
*eedac+ $) 0o. this (ould e the normal res"onse. not an anormal one.
*eedac+ %) 0o. this (ould descrie an overactive chec+"oint. not the underactive one found in "58
mutants
*eedac+ #) Yes. cells (ith #0! damage undergo a"o"tosis. ut this res"onse requires "58.
*eedac+ &) 0o. neither ! nor % are correct.
33@. 9hich statement regarding the actions of glucagon and insulin is *!B'&;
!. Insulin is an anaolic hormone.
$. Glucagon increases levels of c!4P in target cells.
%. Insulin activates a tyrosine +inase.
#. $oth insulin and glucagon ind s"ecifically to "roteins in the "lasma memrane of target cells.
&. Glucagon stimulates glycolysis in target cells.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) It "romotes u"ta+e and storage.
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &) Glucagon inhiits glycolysis y "hos"horylation of "yruvate +inase and P*753.
331. !n en1yme found in the liver ut not in s+eletal muscle is
!. glycogen "hos"horylase.
$. lactate dehydrogenase.
%. "yruvate dehydrogenase.
#. glucose565 "hos"hatase.
&. hexo+inase.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #) 4uscle cannot convert glycogen rea+do(n or gluconeogenesis "roducts into glucose. Biver
can release glucose into the circulation.
*eedac+ &)
333. Phos"horylase a
!. contains "hos"horylated serine residues.
$. exists as a tetramer.
%. is the less active form of the en1yme.
#. is activated directly y !4P.
&. none of the aove
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) increased c!4P 5556 active P7! 5556 active "hos"horylase +inase 5556 active glycogen
"hos"horylase.
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
338. Insulin (ill cause
!. enhanced glucose u"ta+e y the muscle.
$. increased glycogen synthesis.
%. increased oxidation of glucose to caron dioxide and (ater.
#. increased conversion of glucose to fatty acids.
&. all of the aove.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
334. !ll of the follo(ing statements aout "hos"hofructo+inase -P*75 12 are true &?%&PT
!. it is a maDor control en1yme in glycolysis.
$. !TP is a sustrate for P*7.
%. !4P is a negative effector of P*7.
#. !TP is a negative effector of P*7.
&. it cataly1es a metaolically irreversile reactionH i.e.. its equilirium "oint lies far in one direction.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) The committed ste".
*eedac+ $)
*eedac+ %) !4P and fructose53.65is"hos"hate stimulate P*751H !TP and citrate inhiit.
*eedac+ #)
*eedac+ &)
335. In com"arison to the current !merican diet it is recommended that
!. carohydrate consum"tion e reduced and fat consum"tion e increased.
$. that carohydrate consum"tion e increased and fats e decreased.
%. that "rotein consum"tion e decreased.
#. that "rotein consum"tion e increased and fats e increased.
&. that oth carohydrate and fat consum"tion e decreased.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $) L" for deate
*eedac+ %)
*eedac+ #)
*eedac+ &)
336. 9hich is B&!'T li+ely to e characteristic of a regulated en1yme in a metaolic "ath(ay;
!. cataly1es the slo(est ste" of the "ath(ay
$. has a short half5life in vivo
%. concentration is hormonally regulated
#. activity under allosteric control
&. cataly1es a "hysiologically reversile reaction
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &) Irreversile reactions -es"ecially those (ith !TP involvement2 are usually regulated.
33=. Pyridoxal "hos"hate acts as a coen1yme in most
!. transmethylation reactions.
$. caron dioxide fixation reactions.
%. transamination reactions.
#. +inase reactions.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) &ach transaminase has a "yridoxal "hos"hate -$62 "rosthetic grou".
*eedac+ #)
*eedac+ &)
33>. !mmonia enters the urea cycle as
!. free ammonia.
$. free ammonia and caramoyl "hos"hate.
%. glutamine and as"artate
#. as"artate and caramoyl "hos"hate.
&. glutamate and as"artate.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %) Glutamine trans"orts nitrogen in the lood mainly to the liver.
*eedac+ #) The t(o nitrogens that end u" in urea come into the cycle as "art of as"artate and caramoyl
"hos"hate.
*eedac+ &)
33A. :xidation of fatty acids in liver mitochondria may facilitate gluconeogenesis y
!. su""orting the "hos"horylation of !#P.
$. forming acetyl %o! (hich can contriute to the net synthesis of glucose.
%. reducing *!# and 0!#P<.
#. trans"orting camitine into mitochondria.
&. decreasing the de"endence of "hos"horylation of !#P on oxygen consum"tion.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) 4etaolism of fatty acids and resulting acetyl %o! gives higher 0!#, and *!#,3. (hich
leads to increased !TP.
*eedac+ $) ,umans cannot ma+e glucose from acetyl %o!. *ormation of acetyl %o! from "yruvate is a
+ey irreversile reaction.
*eedac+ %)
*eedac+ #)
*eedac+ &) !TP synthesis and :3 consum"tion are cou"led.
38@. 9hich of the follo(ing is a *!B'& statement aout creatine "hos"ho+inase -%P72;
!. %P7 is "resent "redominantly as three different isoen1ymes.
$. %P7 can cataly1e the formation of !TP using creatine "hos"hate and !#P as sustrates.
%. !ll isoen1ymes of %P7 are dimers.
#. !n increase in total serum %P7 is a "ositive indicator of myocardial infarction.
&. !n increase in the serum concentration of one isoen1yme of %P7 aove a certain "ercentage-e.g. AK2
of the total serum %P7 is one indicator of a myocardial infarction.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) True. 44. 4$. and $$ isoen1ymes.
*eedac+ $)
*eedac+ %)
*eedac+ #) 'erum %P7 increases after many ty"es of muscle damage. 4yocardial damage is indicated if
8K or more of the increase in %P7 is the 4$ isoen1yme.
*eedac+ &)
381. The en1yme (hich cataly1es the entrance of acetyl %o! into the citric acid cycle is
!. aconitase.
$. citrate synthase.
%. succinate thio+inase.
#. "yruvate dehydrogenase.
&. isocitric dehydrogenase.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $) %ataly1es) acetyl %o! < oxaloacetate 5556 citrate
*eedac+ %)
*eedac+ #) The P#, com"lex "roduces acetyl %o! from "yruvate.
*eedac+ &)
383. 9hich of the follo(ing is a *!B'& statement aout gluconeogenesis.
!. This anaolic "ath(ay only occurs during "rolonged starvation -days to (ee+s2.
$. This "rocess de"ends on the use of fatty acids as an energy source.
%. This "rocess does not occur in s+eletal muscle.
#. This "rocess is stimulated y citrate.
&. This "rocess requires the use of mitochondrial and cyto"lasmic en1ymes.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) *alse. although critical during starvation it can "lay a role in maintaining lood glucose
et(een normal meals.
*eedac+ $)
*eedac+ %) It occurs in liver -A@K2 and +idney -1@K2.
*eedac+ #) %itrate stimulates fructose51.65is"hos"hatase.
*eedac+ &) Pyruvate caroxylase 55 mitochondria Glucose565"hos"hatase 55 &/ !ll other en1ymes needed
for gluconeogenesis 55 cytosol
388. The "redominant "roducts of anaeroic glycolysis differ from those formed during aeroicglycolysis
ecause...
!. aeroically. lactate diffuses from muscle and is recycled to "yruvate in liver.
$. under aeroic conditions. 0!#, reduces "yruvate to give lactate as the maDor "roduct.
%. 0!# must e re"lenished for glycolysis to continue anaeroically.
#. 0!#, must e re"lenished for glycolysis to continue aeroically.
&. lactate "roduced aeroically (ill e used to reduce 0!#.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) !naeroically. the liver recycles lactate to "yruvate.
*eedac+ $) !naeroically. 0!#, reduces "yruvate to lactate.
*eedac+ %) 9hen :3 is lo( 0!#, cannot e oxidi1ed to 0!#< y oxidative "hos"horylation. 0!#< is
re"lenished y reducing "yruvate to lactate.
*eedac+ #) 0!#< must e re"lenished for glycolysis to continue aeroically or anaeroically.
*eedac+ &) Bactate is "roduced in anaeroic conditions to re"lenish 0!#<.
384. The rate5limiting reaction in urea "roduction is that cataly1ed y
!. argininosuccinase.
$. argininosuccinate synthetase.
%. arginase.
#. ornithine transcaramoylase.
&. caramoyl "hos"hate synthetase.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &) Vust memori1e it.
385. 9hich of the follo(ing is the most accurate com"arison of gluco+inases in muscle and liver;
!. Gluco+inase in oth tissues have aout the same Mmax.
$. Gluco+inases in oth tissues have aout the same 7m.
%. 4uscle gluco+inase has a lo(er Mmax and a lo(er 7m than liver gluco+inase.
#. Biver gluco+inase has a lo(er 7m than the muscle gluco+inase
&. Biver gluco+inase has oth a lo(er Mmax and lo(er 7m than the gluco+inase in muscle.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) 4uscle gluco+inase-hexo+inase2 can cataly1e the "hos"horylation of glucose at lo(er glucose
concentrations. Biver gluco+inase res"onds to higher glucose loads.
*eedac+ #)
*eedac+ &)
386. 9hich of the follo(ing is a *!B'& statement aout oxidative "hos"horylation;
!. This "rocess (ill sto" after !#P is de"leted.
$. :x5"hos requires that "rotons e "um"ed out of the mitochondria matrix.
%. !TP synthesis occurs as "rotons are "um"ed out of the mitochondrial matrix.
#. &lectrons trans"ort (ill continue if 3.45dinitro"henol is added to res"iring mitochondria.
&. !TP synthesis occurs as "rotons enter the mitochondrial matrix through a s"ecific channel.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) This is res"iratory control.
*eedac+ $) ,< is "um"ed from the matrix to the intermemrane s"ace.
*eedac+ %) *alse. !TP in synthesi1ed as "rotons enter the matrix via !TP synthase.
*eedac+ #) True. ut !TP synthesis (ill fall off ecause dinitro"henol is an uncou"ler.
*eedac+ &) The *@ suunit of the !TP synthase is the channel.
38=. The maDor immediate source of urinary ammonia is
!. the hydrolysis of urea y urease.
$. the oxidative dearnination of glutamic acid y glutamate dehydrogenase.
%. the dearnination of histidine y histidine5ammonia lyase.
#. the hydrolysis of glutamine y glutaminase.
&. the oxidative dearnination of amino acids y +idney #5amino acid oxidase.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) %leaves urea to %:3 and 0,8 in the gut.
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
38>. The first "roduct formed during glycogenolysis -glycogen degradation at al"ha 1.4 glycosidiconds2
is...
!. glucose.
$. glucose565"hos"hate.
%. glucose515"hos"hate.
#. galactose.
&. L#P5glucose
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) 'ee %
*eedac+ $) 'ee %
*eedac+ %) glycogen 5556 glucose515"hos"hate 5556 glucose565"hos"hate In the liver glucose565
"hos"hate 5556 glucose 5556 lood glucose
*eedac+ #)
*eedac+ &) L#P5glucose is the immediate sustrate of glycogen synthesis.
38A. !mmonia is not trans"orted in the lood from "eri"heral tissues such as rain in the free state.
Instead. a maDor route for trans"ort of EammoniaE is
!. Glutamine. formed from glutamate as a result of transamination et(een al"ha5+etoglutarate and
ammonia.
$. Glutamate. fonned from ammonium ion and al"ha5+etoglutarate via a reaction involving "yridoxal
"hos"hate as cofactor.
%. Glutamine. formed from glutamate and ammonia via a reaction (hich involves the cofactor 0!#,.
#. Glutamine. formed from glutamate and ammonia via a reaction (hich involves the hydrolysis of !TP.
&. 0one of the other ans(ers is correct.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #) %ataly1ed y glutamine synthase.
*eedac+ &)
34@. The rate of glycolysis is Ecou"ledE to the rate of the citric acid cycle. 9hich com"ound limits
glycolysis so that it dose not exceed the EneedsE of the citric acid cycle;
!. :xaloacetate.
$. Pyruvate.
%. %itrate.
#. 0!#
&. 0!#,
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) %itrate is an inhiitor of "hos"hofructo+inase51. the committed ste" of glycolysis.
*eedac+ #)
*eedac+ &)
341. %yclic !4P de"endent "rotein +inases...
!. are tetrameres com"osed of t(o regulatory and t(o catalytic suunits.
$. are dimers com"osed of one regulatory and one catalytic suunits.
%. "hos"horylate and deactivate "hos"horylase +inase.
#. "hos"horylate and activate glycogen synthase.
&. "hos"horylate the P#, com"lex.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) Protein +inase ! is the s"ecific exam"le.
*eedac+ $)
*eedac+ %) Phos"horylated "hos"horylase +inase is active.
*eedac+ #) Phos"horylated glycogen synthse in inactive.
*eedac+ &) The "yruvate dehydrogenase com"lex is inactive (hen "hos"horylated. ut its
"hos"horylation is mediated y ratios of acetyl %o!J %o!. 0!#,J0!#. and !#PJ!TP. not c!4P.
343. The immediate sustrate used y glycogen synthetase is...
!. L4P5glucose
$. Glucose515"hos"hate
%. Glucose565"hos"hate
#. L#P5glucose
&. Glucose
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) 'ee #
*eedac+ $) 'ee #
*eedac+ %) 'ee #
*eedac+ #) glucose 5556 glucose565"hos"hate 5556 glucose515"hos"hate 5556 L#P5glucose 5556 glycogen
*eedac+ &) 'ee #
348. 'u"eroxide anion is a free radical (hich can e converted to non5radical "roducts y the action of
!. su"eroxide hydrolase.
$. catalase.
%. su"eroxide dismutase -':#2 and catalase.
#. su"eroxide hydrolase and catalase.
&. ferric iron.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) su"eroxide 5556 hydrogen "eroxide 5556 (ater
*eedac+ #)
*eedac+ &)
344. 9hich of the follo(ing is 0:T an accurate com"arison et(een muscle and liver glycogen
"hos"horylase;
!. $oth are increased y cyclic !4P.
$. Glucagon and e"ine"hrine increase glycogen "hos"horylase in oth tissues.
%. %alcium "artially activates muscle glycogen "hos"horylase. ut not glycogen "hos"horylase in liver.
#. 4uscle and liver glycogen "hos"horylase are fully active after "hos"horylation y cyclic!4P de"endent
"rotein +inases.
&. Glycogen "hos"horylase is a monomer in muscle ut exists as a dimer in liver.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $) Glucagon acts on the liver. e"ine"hrine on muscle.
*eedac+ %)
*eedac+ #) Increased c!4P 5556 active "rotein +inase ! 5556 active "hos"horylase +inase 5556 active
glycogen "hos"horylase
*eedac+ &)
345. ! sim"le definition of Eoxidative stressE is
!. it involves the oxidation of iological tissues y free radicals.
$. it al(ays causes cancer.
%. it is the EstressE that follo(s extreme exercise.
#. it descries the over saturation of hemogloin.
&. it results in the formation of methemogloin.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
346. #uring gluconeogenesis. oxaloacetate crosses the inner mitochondrial memrane...
!. after itQs converted to glycerol "hos"hate.
$. y "assive diffusion.
%. after decaroxylation to "yruvate.
#. after reduction to malate.
&. y active trans"ort using !TP as an energy source.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #) 4alate dehydrogenase reduces oxaloacetate to malate in the mitochondria and an isoen1yme
reforms oxaloacetate in the cytosol.
*eedac+ &)
34=. 9hich of the follo(ing forces does 0:T contriute sustantially to the staili1ation of the tertiary
conformation of gloular "roteins;
!. van der 9aals interactions
$. hydrogen onding
%. stac+ing of aromatic rings
#. electrostatic interactions
&. hydro"hoic effect
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
34>. 9hich statement aout the "yruvate dehydrogenase com"lex is *!B'&;
!. ! "roduct of P#, catalysis is acetyl5%o!.
$. P#, is found in the matrix of the mitochondria.
%. 7inase cataly1ed "hos"horylation decreases the activity of P#,.
#. !cetyl %o! and 0!#, oth stimulate P#,.
&. P#, cataly1es a the first reaction (here caron dioxide is formed from glucose.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) Pyruvate < %o! < 0!#< 5556 acetyl %o! < %:3 < 0!#,
*eedac+ $)
*eedac+ %) ! +inase "hos"horylates P#, inactivating itH a "hos"hatase can remove the "hos"hate
reactivating P#,.
*eedac+ #) !cetyl %oa and 0!#, are "roducts of the reaction P#, cataly1es. They cause feedac+
inhiition.
*eedac+ &) 0o %:3 is "roduced y glycolysis.
34A. 9hich is 0:T a common secondary structural elements in gloular "roteins;
!. al"h helices
$. "arallel $eta strands
%. reverse turns
#. tri"le helical undles
&. anti"arallel $eta sheets
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #) %ollagen has a tri"le helix structure and is a firous "rotein.
*eedac+ &)
35@. /educing equivalents formed during totally aeroic glycolysis in a normal liver cell...
!. enter the mitochondria as "rotons.
$. are used in the "entose "hos"hate "ath(ay.
%. are trans"orted into mitochondria in the form of glycerol585"hos"hate.
#. enter the mitochondria as 0!#,.
&. reduce "yruvate to yield lactate and 0!#.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) /educing equivalents donate electrons to the electron trans"ort chain.
*eedac+ $) 0!#P, is "roduced y the ,4P "ath(ay.
*eedac+ %) The glycero"hos"hate shunt.
*eedac+ #) 0!#, cannot cross the mitochondrial memrane.
*eedac+ &) This ha""ens under anaeroic conditions.
351. 9hich of the follo(ing statements does 0:T descrie the structure of gloular "roteins;
!. the surface is hydro"hilic
$. the interior is hydro"hoic
%. "olar side chains are hydrogen onded to other grou"s or (ater
#. side chains are densely "ac+ed (ithin interior
&. reverse turns are uried to "revent solvent contact
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &) 4ost reverse turns are at the surface and consist of hydro"hilic residues.
353. $acteria li+e &. coli can gro( (ith douling times shorter than the amount of time it normally ta+es
to co"y their genome ecause
!. Their genomes are circular. so they do not need telomerase
$. They can reinitiate re"lication efore com"leting a "reviously intiated re"lication cycle
%. They can increase the rate of re"lication for+ "rogression in res"onse to nutrient availaility
#. :nly a small "art of the acterial genome is essential so only "art needs to e du"licated
&. They can activate multi"le origins. decreasing the amount of time it ta+es to co"y the genome
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) This is true. ut irrelevant
*eedac+ $) Yes. y reinitiating efore com"leting a round. acterial cells can overla" re"lication cycles
*eedac+ %) This (ould (or+. ut it isnIt true
*eedac+ #) The entire genome must e accurately du"licated for susequent viaility. so this is not true
*eedac+ &) &u+aryotes use multi"le origins "er chromosome. ut "ro+aryotes -es"ecially those (ith
circular genomes2 do not commonly do this. and &. coli canIt
358. The synthesis of glucose from "yruvate y gluconeogenesis
!. occurs exclusively in the cytosol.
$. is inhiited y an elevated level of glucagon.
%. requires the "artici"ation of iotin.
#. involves lactate as an intermediate.
&. requires the oxidationJreduction of *!#.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) 0o. in the mitochondria. cytosol. and &/.
*eedac+ $) 0o. gluconeogenesis is stimulated y glucagon due to decreased levels of fructose53.65
is"hos"hate.
*eedac+ %) Yes. iotin is a coen1yme that "rovides %:3 to caroxylate "yruvate. forming oxaloacetate.
*eedac+ #) Vust "lain no.
*eedac+ &) /equires 0!#.
354. 9hat is 0:T true of the "e"tide ond
!. limited rotation of the "e"tide ond
$. "lanar
%. "artially charged grou"s
#. ond et(een al"ha caron and caronyl caron
&. resonance staili1ed
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) True due to "artial doule ond character.
*eedac+ $) True due to "artial doule ond character.
*eedac+ %) True due to charged contriuting resonance structures and electronegativity differences.
*eedac+ #) *alse. "e"tide onds are et(een the caronyl caron and the amino nitrogen.
*eedac+ &) True. t(o im"ortant resonance structures
355. 9hich one of the follo(ing is 0:T a characteristic of gluconeogenesis;
!. It requires energy in the form of !TP or GTP.
$. It is im"ortant in maintaining lood glucose during the normal overnight fast.
%. It uses caron s+eletons "rovided y degradation of amino acids.
#. It consists of all the reactions of glycolysis functioning in the reverse direction.
&. It involves the en1yme fructose 1.65is"hos"hatase.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) True. 4 !TP and 3 GTP.
*eedac+ $)
*eedac+ %) 4ost notaly alanine.
*eedac+ #) 0o. the irreversile reactions of glycolysis require unique reactions in gluconeogenesis.
*eedac+ &) This en1yme cataly1es the follo(ing) fructose 1.65is"hos"hate 556 fructose 65"hos"hate.
Phos"hofructo+inase cataly1es the reverse reaction.
356. The sequence of the com"lementary #0! strand for the sequence 5Q5G%T!G%!T!%G!%58Q is)
!. 5Q5%!G%!T!%G!T%G
$. 5Q5%G!T%GT!TG%TG
%. 5Q5GT%GT!TG%T!G%
#. 5Q5G%T!G%!T!%G!%
&. 0one of these are correct
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) This is anti"arallel. ut identical. not com"lementary
*eedac+ $) This is com"lementary. ut not anti"arallel
*eedac+ %) This is oth com"lementary and anti"arallel. and is correct
*eedac+ #) This is identicalH it is neither com"lementary nor anti"arallel
*eedac+ &)
35=. !ll of the follo(ing can directly or indirectly stimulate the activity of muscle glycogen "hos"horylase
exce"tW
!. calcium ions.
$. e"ine"hrine.
%. cyclic !4P.
#. active "hos"horylase +inase.
&. glucagon.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &) Glucagon acts "rimarily on liver and does not affect muscle.
35>. 9hat condition or com"ound does 0:T modulate the extent of oxygen inding in hemogloin;
!. caron dioxide concentration
$. oxygen tension
%. ascorate concentration
#. concentration of 3.85is"hos"hoglycerate
&. ",
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) Increased %:3. decreased oxygen affinity.
*eedac+ $) Increased P:3. increased saturation.
*eedac+ %)
*eedac+ #) Increased $PG -#PG2. decreased oxygen affinity.
*eedac+ &) Increased ,<. decreased oxygen affinity.
35A. *etal hemogloin -,2 inds oxygen (ith greater affinity than adult hemogloin due "rimarily to
(hich fact;
!. the heme *e in fetal , is ferric iron
$. fetal , has a lo(er affinity for 3.85#PG
%. fetal , inds 3 hemes "er suunit
#. fetal , is monomeric
&. fetal , cannot form salt ridges
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
36@. 9hich is most effective in inhiiting the citric acid cycle;
!. fructose53.65is"hos"hate in the mitochondria matrix..
$. a high ratio of !#PJ!TP in the mitochondria matrix.
%. a high ratio of 0!#,J0!# in the mitochondria matrix.
#. a high concentration of citrate in the mitochondria matrix.
&. glycerol585"hos"hate in the matrix.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) *ructose53.65is"hos"hate in the cytosol stimulates "hos"hofructo+inase51 and inhiits
fructose51.65is"hos"hatase.
*eedac+ $) ,igh ratios of !TPJ!#P dam"en T%! cycle.
*eedac+ %) ,igh 0!#,J0!# inactivates P#, and al"ha5+etoglutarate dehydrogenase.
*eedac+ #) ,igh citrate in the cytosol inhiits P*751
*eedac+ &) Glycerol585"hos"hate is a shuttle molecule for reducing equilvalents.
361. 'alt ridges are +ey com"onents in the transition from oxyhemogloin to deoxyhemogloin. 'alt
ridges are im"ortant for (hich reason;
!. 0a%l disru"tion of hydrogen onds in oxyhemogloin
$. &lectrostatic interactions staili1e deoxyhemogloin
%. 0a%l dis"lacement of 3.85#PG in oxyhemogloin
#. *errous salts in hemogloin ind oxygen
&. &lectrostatic interactions enhance the affinity of oxygen and heme
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &) &nhanced affinity aids in transition from deoxy to oxy,. and salt ridges are ro+en.
363. 9hich is a "ositive allosteric effector of "yruvate caroxylase;
!. glucose565"hos"hate
$. acetyl5%o!
%. citrate
#. !#P
&. !TP
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $) !cetyl %o! is an asolute requirement for the catalytic activity of "yruvate caroxylase.
*eedac+ %)
*eedac+ #)
*eedac+ &)
368. The heme5heme coo"erativity in oxygen inding in hemogloin initiates from (hich event;
!. oxygen inding and movement of *e atom into the heme "lane
$. oxidation of three critical cysteine residues in the al"ha chains
%. oxygen com"etitive inding to the 3.85#PG inding site
#. oxygen ridging of t(o adDacent hemes
&. covalent ond formation et(een the four hemes in hemogloin
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) This conformational change is "ro"agated to the other suunits.
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
364. 9hich statement aout "hos"hofructo+inase51 is *!B'&;
!. It is a maDor "oint of control over the rate of glycolysis.
$. !TP is a sustrate.
%. !4P is a negative effector.
#. !TP is a negative effector.
&. It cataly1es a "hysiologically irreversile reaction.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) It cataly1es the committed ste" of glycolysis.
*eedac+ $) !TP < fructose565"hos"hate 5556 fructose51.65is"hos"hate
*eedac+ %) !4P is a "ositive effector.
*eedac+ #)
*eedac+ &)
365. $eta5thalassemia hemogloin is est characteri1ed y (hich of the follo(ing;
!. ra"id oxygen5induced $eta chain degradation
$. no al"ha chains yielding $eta4 tetramers
%. sustitution of a Tyr for a critical "roximal ,is in $eta chains
#. excess al"ha chains cause "athology
&. lo( soluility of $eta chains yielding $eta fiers
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $) al"ha5thalassemia (ith severe anemia -,, disease2.
*eedac+ %)
*eedac+ #) Bittle or no $eta5chains. &xcess al"ha chains "reci"itate.
*eedac+ &)
366. E/es"iratory controlE over oxidative "hos"horylation states that electron flo( and !TPformation sto"
(hen (hich com"ound is asent;
!. !TP
$. !#P
%. 0!#,
#. *!#,
&. oxygen
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $) &lectrons do not ty"ically flo( through electron trans"ort unless !#P is simultaneously
"hos"horylated to !TP.
*eedac+ %) 0!#, and oxygen are required for oxidative "hos"horylation ut res"iratory control is the
need for !#P.
*eedac+ #)
*eedac+ &) 'ee %
36=. 9hat is 0:T true aout the structure of collagen fiers;
!. tro"ocollagen is staili1es as a helical undle of 4 chains
$. hydrogen onds from hydroxyl "rolines are im"ortant
%. "ro"e"tides in each chain are cleaved to form the firils
#. glycines a""ears at nearly every third "osition in the sequence
&. %rosslin+ing of lysine and hydroxylysine residues staili1e the fiers
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) 'u"erhelix of 8 "arallel helical strands.
*eedac+ $)
*eedac+ %) Pro"e"tides are removed from "rocollagen to form tro"ocollagen.
*eedac+ #)
*eedac+ &)
36>. !n en1yme asent in s+eletal muscle is...
!. lactate dehydrogenase.
$. hexo+inase.
%. "yruvate dehydrogenase.
&. glycogen synthetase.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) !naeroic glycolysis
*eedac+ $) glycolysis
*eedac+ %) T%! cycle
*eedac+ #) !n en1yme for gluconeogenesis (hich is carried out in the liver and +idney.
*eedac+ &) Glycogen synthesis.
36A. 9hich statement descries ho( en1ymes cataly1e reactions;
!. en1ymes shift the equilirium constant favoring "roduct formation
$. en1ymes lo(er the activation energy arrier se"arating reactants from "roducts
%. en1ymes destaili1e the transition state y inding more strongly to "roducts
#. en1ymes transfer energy to reactants ma+ing them reactive
&. en1ymes increase the tem"erature of the reaction
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) &n1ymes do not alter equilirium.
*eedac+ $) Lsually y staili1ing intermediates.
*eedac+ %) They staali1e the transition state.
*eedac+ #)
*eedac+ &)
3=@. 4aDor "roducts formed during the "entose "hos"hate "ath(ay are...
!. !TP and 0!#,.
$. /iose and 0!#,.
%. /iose555"hos"hate and 0!#P,.
#. Glucose565"hos"hate and 0!#P,.
&. /iose555"hos"hate and 0!#,.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) /iose555"hos"hate is used for nucleotide synthesis and 0!#P, for fatty acid synthesis.
*eedac+ #) Glucose565"hos"hate and 0!#P are reactants in the ,4P "ath(ay.
*eedac+ &)
3=1. 'erine "roteases contain a catalytic triad im"ortant in catalysis. 9hich statement is true aout the
role of the triad residues;
!. !s" "rotonates the active 'er
$. 'er is the active nucleo"hile
%. Tyrosine "rovides a hydro"hoic "oc+et
#. The covalent intermediate is formed (ith ,is
&. !s" and Tyr form the sustrate inding site
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) !s" staali1es the charged ,is.
*eedac+ $) 'er5:, < ,is 5556 'er5:5 < ,is5,<
*eedac+ %) ,is. !s". and 'er ma+e u" the catalytic triad.
*eedac+ #) 'erine forms a covalent ond to the "e"tide.
*eedac+ &) 'ee %.
3=3. The ultimate effect of cyclic !4P on liver "hos"hofructose +inase53 -P*7532 is...
!. that it "hos"horylates P*753 (hich increases its "hos"hatase activity and slo(s glycolysis.
$. that it de"hos"horylates P*753 (hich increases its "hos"hatase activity and slo(s glycolysis.
%. that it increases the concentration of fructose53.65is"hos"hate.
#. enhances !TP inhiition of P*751.
&. decreases !TP inhiition of P*753.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) increased glucagon 5556 increased c!4P 5556 "hos"horylated P*753 5556 decreased fructose5
3.65is"hos"hate 5556 slo(s glycolysis.
*eedac+ $) #e"hos"horylated P*753 is a +inase that cataly1es) fructose 565"hos"hate 5556 fructose 53.65
is"hos"hate (hich stimulates P*751.
*eedac+ %) 'ee !
*eedac+ #) ,igh levels of fructose53.65is"hos"hate can overcome inhiition of P*751 y !TP.
*eedac+ &) 'ee #
3=8. In noncom"etitive +inetics. (hat is the effect of excess sustrate;
!. "revents inding of the inhiitor
$. falls to alter the effect of the inhiitor
%. yields maximal velocity
#. excess sustrate maximi1es the inhiitory effect of the inhiitor
&. increases 7m
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) 'ee $.
*eedac+ $) $ecause the inhiitor inds to a site different from the sustrate inding site. the level of
sustrate does not affect the inhiitors inding.
*eedac+ %) Mmax in decreased.
*eedac+ #)
*eedac+ &) 7m is unchanged.
3=4. The Ecommitted ste"E of the citric acid cycle involves the conversion of...
!. oxaloacetate to citrate.
$. the conversion of citrate to isocitrate.
%. the conversion of isocitrate to al"ha +etoglutarate.
#. the conversion of fumarate to malate.
&. the conversion of succinyl5%o! to succinate.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) This reaction is regulated and essentially irreversile. ut not the committed ste".
*eedac+ $) ! reversile reaction
*eedac+ %) This decaroxylation is essentially irreversile. The reaction is stimulated y !#P and
inhiited y !TP.
*eedac+ #) ! reversile reaction
*eedac+ &) ! reversile reaction.
3=5. 9hat est descries the 7m term in 4ichaelis54enton +inetics;
!. sustrate concentration that yields maximal velocity
$. the reaction rate L of rea+do(n of the &' com"lex to "roduct
%. a ratio of rate constants -+3<+82J 71
#. the concentration of active en1yme
&. a thermodynamic constant unique for the given en1yme
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) 'ustrate concentration that yields 1J3 Mmax.
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
3=6. %oen1yme T is unique trans"orter of electrons during oxidative "hos"horylation ecause...
!. it is freely moile in the hydro"hoic inner mitochondrial memrane.
$. it is the "oint (here cyanide interu"ts electron tran"ort.
%. it can directly acce"t electron from oth *!#, and 0!#,.
#. it is the only "art of the electron trans"ort chain that is solule.
&. it is the final donor of electron to reduce molecular oxygen.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) !lso called uiquinone. it transfers electrons from com"lexes I and II to com"lex III.
*eedac+ $) %yanide. a1ide. and caron monoxide all inhiit electron trans"ort at the a8 of com"lex IM.
*eedac+ %) &lectrons are transferred from 0!#, through com"lex I and from *!#,3 through com"lex II
to uiquinone.
*eedac+ #)
*eedac+ &) %ytochrome aJa8 is the final electron donor.
3==. /es"iratory "oisons li+e cyanide and caron monoxide act y...
!. disru"ting the inner mitochondrial memrane.
$. com"lexing the the irons of cytochromes.
%. "reventing !#P from interacting (ith inorganic "hos"hate.
#. interfering (ith the trans"ort of oxygen into the matrix of mitochondria.
&. inhiiting !TP synthetase.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $) %yanide and a1ide ind to the ferric form of a8. caron monoxide inds to the ferrous form.
*eedac+ %)
*eedac+ #)
*eedac+ &)
3=>. 9hich t(o com"ounds (ill increase *I/'T in liver follo(ing a ra"id increase in circulating glucagon;
!. "yruvate and oxaloacetate
$. "yruvate and c!4P
%. c!4P and glucose 15"hos"hate
#. oxaloacetate and c!4P
&. glucose 15"hos"hate and oxaloacetate
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) Glucagon inding to its rece"tor increases cytosolic c!4P and causes glycogen rea+do(n to
glucose515"hos"hate.
*eedac+ #)
*eedac+ &)
3=A. 0!#P, for fatty acid synthesis is directly su""lied y
!. isocitrate dehydrogenase.
$. glycogen "hos"horylase.
%. al"ha5+etoglutarate dehydrogenase.
#. glucose565"hos"hate dehydrogenase.
&. the transfer of reducing "o(er from 0!#, to 0!#P in mitochondria.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) ! T%! cycle en1yme that does not use or "roduce 0!#P,.
*eedac+ $) #egradation of glycogen. does not use or "roduce 0!#P,.
*eedac+ %) Produces 0!#,.
*eedac+ #) ,4P "ath(ay. su""lies 0!#P, and riose555"hos"hate for synthesis of other iomolecules.
*eedac+ &) 0!#, is the maDor reducing equivalent in the mitochondria and 0!#P, "redominates in the
cytosol.
3>@. Increased levels of !TP in the fed state hel"s to channel acetyl %o! into fat synthesis y inhiiting
!. citrate synthase.
$. isocitrate dehydrogenase.
%. citrate lyase.
#. acetyl %o! caroxylase.
&. "almitate thio+inase -%o! synthase2.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) Inhiited y high !TP ut no a significant rate limiting ste".
*eedac+ $) The committed ste" of T%! cycle is inhiited so acetyl %o! is not eing used u" y T%! cycle
and citrate accumulates.
*eedac+ %) This en1yme is needed for fatty acid synthesis.
*eedac+ #) 0eeded for fatty acid synthesis.
*eedac+ &)
3>1. !n im"ortant "roduct of the "entose "hos"hate "ath(ay is
!. riose "hos"hate.
$. !TP
%. 0!#P
#. !#P
&. 0!#,
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) /iose555"hos"hate is uesed in nucleotide synthesis. 0!#P, is another im"ortant "roduct.
*eedac+ $) !TP is not used or "roduced in this reaction.
*eedac+ %) 0!#P,
*eedac+ #)
*eedac+ &) 0!#P,
3>3. 'ustrates in the P&0T:'& P,:'P,!T& P!T,9!Y include
!. 0!#P, < glucose.
$. glucose < 0!#.
%. glucose565"hos"hate < 0!#.
#. glucose565"hos"hate < 0!#P.
&. riose555"hos"hate < 0!#.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) glucose565"hos"hate < 30!#P < ,3: 5556 riose555"hos"hate < 30!#P, < 3,< < %:3.
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
3>8. 9hich of the follo(ing is *!B'& aout a "erson (hose s+eletal muscle is unale to "erform
glycolysis;
!. They (ill de"end almost totally on fatty acid oxidation as an energy source during exercise.
$. Gluconeogenesis (ill su""ly glucose to su""ort active exercise.
%. They (ill li+ely have hy"eruricemia after a "eriod of exercise.
#. They (ill require an overload of glucose efore and during exercise.
&. They (ill exhiit considerale exercise intolerance.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $) It is of no use to su""ly glucose ecause the muscle cannot "erform glycolysis to otain
energy from the glucose. # is also false.
*eedac+ %)
*eedac+ #) YouQre right. ut also see $.
*eedac+ &)
3>4. &levated levels of circulating glucagon are associated (ith (hich one of the follo(ing;
!. Increased activity of "hos"hofructo+inase53
$. #ecreased level of fructose 3.65is"hos"hatase activity
%. #ecreased fructose51.65is"hos"hatase activity
#. *asting
&. Ingestion of a carohydrate5rich meal
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) Incorrect. ecause in liver +inase activity is highest for de"hos"ho5P*753. and glucagon leads
to "hos"horylation of the P*753.
*eedac+ $) Incorrect ecause "hos"hatase activity is highest for "hos"ho5P*753. so glucagon (ould
increase activity.
*eedac+ %) Increased activity ecause glucagon "romotes gluconeogenesis.
*eedac+ #) Glucagon "romotes glycogenolysis and gluconeogenesis to maintain adequate lood sugar
levels et(een meals.
*eedac+ &) Glucose is asored and lood glucose levels rise. so insulin is needed to "romote cell u"ta+e
of glucose.
3>5. 9hich amino acid is 0:T ioni1ed at "hysiological ",;
!. glutamate
$. arginine
%. serine
#. lysine
&. as"artate
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) %onDugate ase. negative charge
*eedac+ $) $ase. "ositive charge
*eedac+ %) Polar and can e ioni1ed. ut not at "hysiological ",.
*eedac+ #) $ase. "ositive charge
*eedac+ &) %onDugate ase. negative charge
3>6. 9hich one of the follo(ing statements concerning glutamine is I0%://&%T;
!. Glutamine is res"onsile for the trans"ort and storage of ammonia in a nontoxic form.
$. The only fate of glutamine is hydrolysis to glutamate and ammonia.
%. !TP is required for the reaction leading to the synthesis of glutamine from glutamate and ammonia.
#. The +idneys can hydroly1e glutamine to glutamate and ammonia.
&. Glutamine is found in tissue "roteins.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) Glutamine trans"orts ammonia from tissues to the liver (here urea is "roduced.
*eedac+ $) Incorrect ecause glutamine is also used in the sythesis of "urines. "yrimidines. and
"roteins.
*eedac+ %) Glutamate < 0,4< < !TP 556 glutamine < !#P
*eedac+ #) Glutaminase is found in +idney. although most glutamine is hydroly1ed in the liver.
*eedac+ &) Glutamine is one of the 3@ asic amino acids.
3>=. 'atellite sequences in human cells
!. are re"eated sequences (hose density is different from the ul+ of the genome
$. are extrachromosomal elements found in cells that have am"lified "articular genes
%. are re"eated sequences that are inters"ersed throughout the genome
#. ma+e u" less than 1K of the total genomic #0! of humans
&. are thought to e EDun+E #0! (ithout any ovious function
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) This is the definition of a satellite sequence
*eedac+ $) 'uch things exist ut are called e"isomes or doule minutes. not satellites
*eedac+ %) 'atellites are re"eated. ut are clustered in tandem re"eats. such as the al"ha5satellites in
humans found near centromeres
*eedac+ #) To e detected as a satellite. a sequence must e "resent enough times to create a
noticeale alteration of the #0! "rofile in a cesium chloride gradientH 1K is not enough
*eedac+ &) The al"ha satellite in humans has een associated (ith centromere function. and telomeric
re"eats have een found to e needed for telomere function.
3>>. 9hich one of the follo(ing statements aout the urea cycle is correct;
!. The t(o nitrogen atoms that are incor"orated into urea enter the cycle as ammonia and alanine.
$. Lrea is "roduced directly y the hydrolysis of ornithine.
%. !TP is required for the reaction in (hich argininosuccinate is cleaved to form arginine.
#. Lrinary urea is increased y a diet rich in "rotein.
&. The urea cycle occurs exclusively in the cytosol.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) The t(o nitrogen atoms come from ammonia and as"artate.
*eedac+ $) ,ydrolysis of arginine.
*eedac+ %) Vust "lain no.
*eedac+ #) True ecause there is no real storage form for amino acids. so excess amino acids are
metaoli1ed. (ith the caron chains eing used for energy and the nitrogen removed through urea.
*eedac+ &) 4itochondria and cytosol.
3>A. 9hich is 0:T true as to (hy glycine is a unique amino acid;
!. no caron side chain
$. commonly found in reverse turns
%. more diverse "hi."si angles "ossile than other residues
#. ty"ically found every third residue in collagen
&. "refers cis5"e"tide ond
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) True. the / grou" is a hydrogen.
*eedac+ $) True. no side5chain hindrance allo(s unusual dihedral angles.
*eedac+ %) True. no side5chain hindrance allo(s unusual dihedral angles.
*eedac+ #) True. In the collagen tri"le helix structure every 8rd residue faces the cro(ded center. only
Gly (ill fit ecause it has no caron side5chain.
*eedac+ &) *alse. In all cis "e"tides mutual hindrance et(een neighoring side5chains is severe.
3A@. 9hich one of the follo(ing statements aout the synthesis of caramoyl "hos"hate y caramoyl
"hos"hate synthetase I is I0%://&%T;
!. The en1yme cataly1es the rate5limiting reaction in the urea cycle.
$. The reaction is allosterically activated y 05acetylglutamate.
%. The reaction requires t(o high5energy "hos"hates for each caramoyl "hos"hate molecule synthesi1ed.
#. The en1yme incor"orates %:3 into caramoyl "hos"hate.
&. The reaction is reversile.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) 'ee &.
*eedac+ $) 'ee &.
*eedac+ %) 'ee &.
*eedac+ #) %:3 < 0,4< < 3!TP 556 caramoyl "hos"hate < 3!#P.
*eedac+ &) 9hen !TP is used to drive a reaction the reaction is essentially irreversile and usually
regulated.
3A1. 'ynthesis of dT4P in human cells is inhiited y administering
!. 55fluorouracil
$. 55fluoroadenine
%. 55fluoroguanine
#. 55fluorocytosine
&. 55fluorothymidine
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) Yes. this is "rocessed to *5dL4P (hich is a suicide inhiitor of thymidylate synthase
*eedac+ $) 'ee the note for choice !
*eedac+ %) 'ee the note for choice !
*eedac+ #) 'ee the note for choice !
*eedac+ &) 'ee the note for choice !
3A3. In (hich one of the follo(ing tissues is glucose trans"ort into the cell enhanced most y insulin;
!. $rain
$. Bens
%. /ed lood cells
#. !di"ose tissue
&. Biver
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) 'ee #.
*eedac+ $) 'ee #.
*eedac+ %) 'ee #.
*eedac+ #) '+eletal muscle and adi"ocytes are de"endent on insulin for glucose u"ta+e. 0ervous tissue.
he"atocytes. /$%Is. cornea are insulin inde"endent.
*eedac+ &) 'ee #.
3A8. 9hich modification reaction is 0:T im"ortant in directing memrane association;
!. myristylation
$. "almitolytion
%. !#P5riosylation
#. iso"renylation
&. "hos"hoinositol5glycan
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) *atty acid addition. highly li"id solule
*eedac+ $) *atty ester addition. highly li"id solule
*eedac+ %) 4odification from 0!#. not very li"id solule or normally "art of memranes.
*eedac+ #) Polyiso"rene addition. highly li"id solule
*eedac+ &) Glycoli"id addition
3A4. Insulin does all of the follo(ing &?%&PT
!. enhance glucose trans"ort into muscle.
$. enhance glycogen formation y liver.
%. increase li"olysis in adi"ose tissue.
#. inhiit gluconeogenesis in liver.
&. enhance amino acid trans"ort into muscle.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) 'ee %.
*eedac+ $) 'ee %.
*eedac+ %) Insulin is high in the fed5state and "romotes u"ta+e and storage of nutrients. Bi"olysis -fat
rea+do(n2 occurs (hen glucagon is high.
*eedac+ #) Gluconeogenesis is stimulated y glucagon.
*eedac+ &) 'ee %.
3A5. BI0&s are 0:T
!. !out 6 +" elements
$. *ound ty"ically in loc+s of tandem re"eats
%. !le to encode reverse transcri"tase
#. *ound in the human genome
&. /etrotrans"osons
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) The si1e of individual elements varies. ut an intact element is aout 6@@@ "
*eedac+ $) BI0&s are trans"osons that are distriuted throughout the genome -the FIG is for
Finters"ersedG2.
*eedac+ %) 0ot all elements still encode active en1yme. ut some do so the class of elements is ale to
encode /T
*eedac+ #) BI0&s are not limited to humans. ut are found in humans
*eedac+ &)
3A6. 9hich one of the follo(ing is 0:T a direct action of insulin inding to the cell memrane;
!. !ctivation of tyrosine +inase activity of the 5suunit of the insulin rece"tor
$. Phos"horylation of the intracellular domain of the insulin rece"tor
%. Phos"horylation of intracellular "roteins
#. !ctivation of adenylate cyclase
&. Increased activity of and numer of glucose trans"ort molecules in the cell memrane
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $) !uto"hos"horylation.
*eedac+ %) The covalent modification changes the activity of en1ymes.
*eedac+ #) !denylate cyclase can e activated u"on rece"tor inding of either glucagon or e"ine"hrine.
ut the insulin rece"tor is a tyrosine +inase.
*eedac+ &) To ring aout increased glucose u"ta+e.
3A=. 'ide chain amino acid modifications commonly occur)
!. to amino acids "rior to charging of the t/0!
$. to the amino acyl5t/0! com"lex
%. to riosome ound "re"rotein chains
#. to nascent or com"leted "oly"e"tide chains
&. "roteins "re5attached to the &/ memrane
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #) 4ostly "roteins are made according to the m/0! tem"late. then modified (hen com"letely
translated -"ost5translational modification2.
*eedac+ &)
3A>. 4uscle glycogen cannot contriute directly to lood glucose levels ecause
!. muscle glycogen cannot e converted to glucose 65"hos"hate.
$. muscle lac+s glucose 65"hos"hatase.
%. muscle contains no gluco+inase.
#. muscle contains no glycogen "hos"horylase.
&. muscle lac+s "hos"hoglucoisomerase.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) *alse. see $.
*eedac+ $) 4uscle can rea+do(n stored glycogen to glucose565"hos"hate ut lac+s glucose565
"hos"hatase. so it cannot "roduce glucose.
*eedac+ %) True. ut gluco+inase "hos"horylates glucose to glucose565"hos"hate. aiding in removal of
glucose from the lood.
*eedac+ #) Vust "lain no. 4uscle does have this en1yme to rea+do(n stored glycogen.
*eedac+ &)
3AA. If one strand of a 1@ +" du"lex #0! molecule has 8@@@ G residues. the overall G<% content of the
du"lex is
!. 15K
$. 8@K
%. 45K
#. 6@K
&. There is not enough information to determine the ans(er
'ho( ans(er
%orrect !ns(er) &
*e
edac+ !) 'ee the note for choice F&GH this value is elo( the minimum "ossile for the information given.
*eedac+ $) 'ee the note for choice F&GH this is the minimum "ossile value. ut it could e higher
*eedac+ %) 'ee the note for choice F&G
*eedac+ #) 'ee the note for choice F&G
*eedac+ &) If one strand has 8@@@ Gs. the other strand has 8@@@ %s. ut the total G<% content is
undetermined since the first strand could have @5=@@@ %s. 'o the G<% content is a minimum of 8@K. ut
could e as high as 1@@K. 4ade you thin+. though. didnIt I;
8@@. 9hich one of the follo(ing is 0:T characteristic of the hexose mono"hos"hate "ath(ay;
!. It "roduces %:3.
$. It is controlled y inhiition of glucose565"hos"hate dehydrogenase y 0!#P,.
%. In requires !TP for "hos"horylation.
#. It "roduces riose 55"hos"hate.
&. It involves the rea+age and formation of %5% onds.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) 6 caron glucose565"hos"hate looses %1 to ecome riulose555"hos"hate. a 5 caron sugar.
*eedac+ $) *eedac+ inhiition.
*eedac+ %) 0o !TP is consumed or "roduced.
*eedac+ #) 'ee !.
*eedac+ &) 'ee !.
8@1. 'curvy arises from the failure of (hich "ost5translational modification;
!. hydroxylation of Pro
$. hydroxylation of Bys
%. gamma5caroxylation of Glu
#. '5nitrosylation of %ys
&. 05terminal myristylation
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) Bac+ of vitamin % leads to an inaility to hydroxylate Pro. and thus collagen cannot form the
a""ro"riate ,5onds to ma+e firils.
*eedac+ $) ,ydroxyBys is common in collagen. ut not invloved (ith scurvy.
*eedac+ %)
*eedac+ #)
*eedac+ &)
8@3. 9hich one of the follo(ing reactions does 0:T consume or "roduce 0!#P,;
!. /eduction of oxidi1ed glutathione
$. 'ynthesis of steroids
%. %onversion of glucose 65"hos"hate to 65"hos"hogluconolactone
#. 4icrosomal hydroxylation (ith the cytochrome P545@ oxygenase system
&. :xidative "hos"horylation
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) Glutathione reductase cataly1es the follo(ing reaction) G5'5'5, < 0!#P, < ,< 5556 3G5',
< 0!#P<
*eedac+ $) #esmolase cataly1es) cholesterol < 0!#P, < :3 5556 "regnenolone < 0!#P<
*eedac+ %) *irst ste" in the hexose mono"hos"hate "ath(ayH "roduces 0!#P,.
*eedac+ #) %ytochrome P545@ cataly1es) /5, < :3 < 0!#P, < ,< 5556 /5:, < ,3: < 0!#P<
*eedac+ &) 0!#, and *!#,3-not 0!#P,2 su""ly electrons to the electron trans"ort chain.
8@8. 0ucleosome cores
!. contain aout 8@@ " of #0!
$. contain #0! that is more sensitive to nuclease digestion than lin+ers et(een nucleosomes
%. are staili1ed y histone ,1
#. contain 3 co"ies of the histone ,3!
&. are found "redominantly near centromeres and telomeres
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) ! nucleosome core has 146 " of #0!
*eedac+ $) The #0! et(een nucleosome cores. the lin+er #0!. is more sensitive to nuclease digestion
than the #0! in the core.
*eedac+ %) ,1 staili1es the 8@ nm fiers that are formed y interactions among adDacent nucleosome
cores. ,1 is not "art of the core nucleosome.
*eedac+ #) Yes. as (ell as 3 co"ies each of ,3$. ,8. and ,4.
*eedac+ &) Mirtually all #0! in a eu+aryotic cell is incor"orated into nucleosomesH if anything they are
less "rominent at s"ecific structures li+e these ecause other "rotein com"lexes are found in these areas.
8@4. 9hich one of the follo(ing conditions decreases the oxidation of acetyl %o! y the citric acid cycle;
!. ! lo( !TPJ!#P ratio
$. Bo( 0!#, due to ra"id oxidi1ation to 0!#< through the res"iratory chain
%. ! lo( 0!#<J0!#, ratio
#. ,igh concentration of !4P
&. Bo( GTPJG#P ratio
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) 9hen !TP is lo(. "yruvate dehydrogenase com"lex is activated. and more acetyl %o! is "ut
into T%! cycle. %itrate synthase. isocitrate dehydrogenase. and al"ha5+etoglutarate dehydrogenase are
also activated (hen !TP is lo(.
*eedac+ $) 'ee %.
*eedac+ %) Pyruvate dehydrogenase com"lex is in the inactive form (hen "hos"horylated. The +inase.
(hich "hos"horylates the P#%. is active (hen %o!Jacetyl %o! or 0!#<J0!#, ratios are lo(.
*eedac+ #)
*eedac+ &) ,igh GTP inhiits al"ha5+etoglutarate dehydrogenase.
8@5. 9hich is 0:T true aout structures of gloular "roteins;
!. "ac+ing density of nearly =5K
$. surface hydrated (ith (ater molecules
%. "e"tide ond caronyl and amide grou"s hydrogen onded
#. tertiary structures consist of layers of secondary structures
&. strong hydro"hoic onds in reverse turns
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) True. 'ee $
*eedac+ $) True. The inner "ortion has "ac+ed hydro"hoic residues and the surface has more
hydro"hilic residues.
*eedac+ %) True. ma+ing al"ha helices and eta sheets
*eedac+ #) True
*eedac+ &) *alse. turns are usually near the surface and hydro"hilic.
8@6. !n uncou"ler of oxidative "hos"horylation such as dinitro"henol
!. inhiits electron trans"ort and !TP synthesis.
$. allo(s electron trans"ort to "roceed (ithout !TP synthesis.
%. inhiits electron trans"ort (ithout im"airment of !TP synthesis.
#. s"ecifically inhiits cytochrome .
&. acts as a com"etitive inhiitor of 0!#<5requiring reactions in the mitochondrion.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) 'ee $.
*eedac+ $) ,< ions are eing "um"ed from the matrix side to the cytosolic side of the inner
mitochondrial memrane. ut the uncou"lers transfer ,< ac+ to the matrix side y"assing the !TP
synthase.
*eedac+ %) 'ee $
*eedac+ #) 'ee $
*eedac+ &) 'ee $
8@=. ! mutated virus is found to re"licate its genome faster than it used to. It is li+ely that it no( also
!. has a faster rate of transcri"tion
$. has a larger genome. since it can co"y more #0! in the same amount of time
%. has a higher mutation frequency
#. is more resistant to antiiotics
&. has a narro(er host s"ecificity
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) The rates of transcri"tion and re"lication are largely inde"endent
*eedac+ $) ! larger genome (ould ta+e longer to co"y. 'ince the mutation rate is "roaly higher no(
-see F%G2 the mutational load is higher. and the genome is not li+ely to get larger.
*eedac+ %) YesH less accuracy is a common consequence of faster re"lication. Ty"ically. the #0!
"olymerase s"ends less time determining (hether the most recent catalytic cycle (as accurate. so it goes
faster ut ma+es more mista+es.
*eedac+ #) If (e inter"ret FantiioticsG roadly enough to include FantiviralsG. a virus (ith a higher
mutation rate -see choice %2 could acquire resistance at a higher frequency. ut this (ould have to e an
indirect consequence of the direct effect of higher mutation rates. 'o % is a etter ans(er.
*eedac+ &) 9ho +no(s. I needed a fifth ans(er and this sounded li+e it could ha""en. or (ould at least
ma+e you thin+ aout it.
8@>. Gluco+inase
!. is (idely distriuted and occurs in most mammalian tissues.
$. has a high 7m for glucose and. hence. is im"ortant in the "hos"horylation of glucose "rimarily after
ingestion of a carohydrate5rich meal.
%. is inhiited y glucose 65"hos"hate.
#. levels are decreased y carohydrate5rich diets.
&. cataly1es a readily reversile reaction.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) Gluco+inase is found is liver and $5cells. ,exo+inase is (idely distruuted.
*eedac+ $) ,exo+inase has a lo( 7m and "hos"horylates glucose (hen glucose levels are much lo(er.
*eedac+ %) ,exo+inase is inhiited y glucose5 65"hos"hate. ut not gluco+inase.
*eedac+ #) ,igh carohydrate consum"tion increases the amount of gluco+inase.
*eedac+ &) The reaction involves the transfer of a high energy "hos"hate from !TP and is regulated and
essentially irreversile.
8@A. The al"ha helix and the collagen helix differ in many (ays. 9hich of the follo(ing statements in 0:T
true in ho( they differ;
!. al"ha helix is more elongated than the collagen helix im"lying a greater rise "er residue
$. the al"ha helix consists of a single "oly"e"tide chain unli+e the tri"le stranded helix in collagen
%. hydrogen onding in the al"ha helix is (ithin a chain unli+e hydogen onding et(een chains in the
collagen helix
#. all amide and caronyl grou"s are hydrogen onded to other residues (ithin the al"ha helix instead of
some hydrogen onding to solvent in the collagen helix
&. al"ha helices are usually limited to three helical turns. (hereas the collagen helix extends much longer
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) *alse. the collagen helix is more elongated (ith a rise "er residue of 3.A com"ared to a rise
"er residue of 1.5 for an al"ha helix.
*eedac+ $) True
*eedac+ %) True
*eedac+ #) True
*eedac+ &) True
81@. The reaction cataly1ed y "hos"hofructo+inase
!. is activated y high concentrations of !TP and citrate.
$. uses fructose515"hos"hate as a sustrate.
%. is the rate5limiting reaction of the glycolytic "ath(ay.
#. is near equilirium in most tissues.
&. is inhiited y fructose 3.65is"hos"hate.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) P*751 is inhiited y high !TP and citrate.
*eedac+ $) 0o. the reaction is) fructose565"hos"hate 5556 fructose5 1.65di"hos"hate.
*eedac+ %) Yes. it is the committed ste" of glysolysis.
*eedac+ #)
*eedac+ &) *ructose53.65is"hos"hate and !4P activate P*751.
811. $efore cataly1ing the incor"oration of a nucleotide into a gro(ing #0! chain. #0! "olymerase chec+s
for
!. the a""ro"riate formation of hydrogen onds et(een the incoming ase and the tem"late ase
$. the formation of stac+ing interactions et(een the incoming ase and the adDacent "rimer ase
%. the asence of rare tautomeric shifts in the incoming ase that can alter ase "airing
#. solvent access of the catalytic site to ensure the ra"id esca"e of "yro"hos"hate after the reaction
&. the "ro"er distance et(een the incoming al"ha "hos"hate and the tem"late "hos"hodiester grou"
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) 'ounds reasonale. and you may even have een told this efore. ut it Dust isnIt true and I
tried to ma+e this clear in my class.
*eedac+ $) 'tac+ing or hydro"hoic interactions are very im"ortant energetically. ut have no s"ecificity
and are not a concern of #0! "olymerase.
*eedac+ %) Polymerase is not ca"ale of "erforming this chec+. (hich is (hy it ma+es most of the
mista+es it ma+es.
*eedac+ #) 'ounds im"ortant. made it u".
*eedac+ &) :dd. ut true. 0ucleotide analogs inca"ale of hydrogen onding. ut (ith the right sha"e.
are incor"orated y #0! "olymerase.
813. %om"ared to the resting state. vigorously contracting muscle sho(s
!. an increased conversion of "yruvate to lactate.
$. decreased oxidation of "yruvate to %:3 and (ater.
%. a decreased 0!#,J0!#< ratio.
#. decreased concentration of !4P.
&. decreased levels of fructose 3.65is"hos"hate.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) FMigorouslyG is the +ey (ord here. The muscle has a high energy demand that is not eing
met y oxidative "hos"horylation so anaeroic glycolysis increases.
*eedac+ $) 0o. the cell is using glycolysis and T%! cycle to fuel oxidative "hos"horylation. so "yruvate
oxidation increases.
*eedac+ %) 0o. ecause glycolysis and T%! cycle -if aeroic2 are "roducing more 0!#,.
*eedac+ #) Increased !#P and !4P ecause !TP is eing de"hos"horylated.
*eedac+ &)
818. 9hich does 0:T contriute to staility of the al"ha helix;
!. hydrogen onding across diameter of helix
$. stagger of side chains "ointing out(ard from helix axis
%. van der (aals contact across the helix diameter
#. aligned hydrogen onds of amides and caronyl oxygens
&. "ac+ing against neighoring secondary structural elements
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) *alse. ,5onding is "arallel to the axis of the helix.
*eedac+ $) True. decreases side5chain hindrance.
*eedac+ %) True
*eedac+ #) True. 'ee !
*eedac+ &) True
814. 9hich one of the follo(ing statements concerning gluconeogenesis is correct;
!. It occurs in muscle.
$. It is stimulated y fructose53.65is"hos"hate.
%. It is inhiited y elevated levels of acetyl %o!.
#. It is im"ortant in maintaining lood glucose during the normal overnight fast.
&. It uses caron s+eletons "rovided y degradation of fatty acids.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) Gluconeogenesis occurs A@K in the liver and 1@K in +idney.
*eedac+ $) P*751. and therefore glycolysis. is stimmulated y fructose53.65is"hos"hate.
*eedac+ %) The "yruvate dehydrogenase com"lex is the en1yme inhiited y high acetyl %o!. !cetyl %o!
is essential for "yruvate caroxylase in the first ste" of gluconeogenesis.
*eedac+ #)
*eedac+ &) The caron s+eletons come from amino acids.
815. #uring renaturation of se"arated nucleic acid strands. the slo(est ste" in the "rocess is
!. Bo(ering the tem"erature to the "ro"er range
$. Bo(ering the ", to the "ro"er range
%. The initial contact et(een t(o small com"lementary "atches
#. &xtension of the initial contact to adDacent regions -E1i""eringE2
&. &stalishment of the hy"ochromic shift.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) This is very ra"id
*eedac+ $) This very ra"id
*eedac+ %) Yes. contact is slo(. determined y concentration of the "artners. and rate5limiting
*eedac+ #) This is fast. see %
*eedac+ &) The hy"ochromic shift is an instantaneous consequence of the ase stac+ing that occurs
during annealing
816. In human liver. the initial ste" in the utili1ation of fructose is its "hos"horylation to fructose 15
"hos"hate. This is follo(ed y
!. "hos"horylation to fructose 1.65is"hos"hate.
$. cleavage of fructose 15"hos"hate to form glyceraldehyde and dihydroxyacetone "hos"hate.
%. conversion to fructose 65"hos"hate y action of a "hos"hofructomutase.
#. isomeri1ation to glucose 15"hos"hate.
&. hydrolysis to fructose follo(ed y isomeri1ation to glucose.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) This is the fate of fructose 65"hos"hate in glycolysis.
*eedac+ $) %ataly1ed y aldolase $.
*eedac+ %) Phos"hoglucomutase isomeri1es glucose 65"hos"hate and glucose 15"hos"hate in glycogen
synthesis and degradation.
*eedac+ #) 'ee %.
*eedac+ &) Vust "lain no.
81=. 9hich is 0:T an im"ortant allosteric regulators of hemogloin oxygenation;
!. hydrogen ion concentration
$. %: concentration
%. chloride
#. #PG
&. %:3 concentration
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) increased N,<O 5556 decreased :3 affinity
*eedac+ $) %: inds at the same site as :3. and is thus not an allosteric interaction ut a com"etative
interaction.
*eedac+ %) 'taili1es the al"ha chains in deoxyhemogloin.
*eedac+ #) increased #PG 5556 decreased :3 affinity
*eedac+ &) increased N%:3O 5556 decreased :3 affinity
81>. The en1yme in muscle (hich is most directly stimulated y e"ine"hrine is
!. glycogen synthase.
%. isocitrate dehydrogenase.
&. adenylate cyclase.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) This en1yme is inactivated due to e"ine"hrine5induced "hos"horylation.
*eedac+ $) Boss of stimmulation due to e"hine"hrine5 induced decreases in the level of fructose 3.65
is"hos"hate.
*eedac+ %) Indirectly affected.
*eedac+ #) This en1yme is found in liver and +idney and is involved in gluconeogenesis.
*eedac+ &) &"hine"hrine inding to its rece"tor activates adenylate cyclase.
81A. The est evidence that #0! carries genetic information is
!. it can transform the "ro"erties of cells in heritale (ays
$. it can e du"licated using the information in either strand
%. it is a chemically stale "olymer
#. it com"rises most of the material inDected into cells y some viruses
&. information in #0! is found to e co"ied into /0!
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) This is not only the est ex"eriment in terms of clean results. it is conce"tually the real
evidence that #0! carries genetic information. ecause it sho(s that genetic information is altered y
changing the #0!.
*eedac+ $) True. and useful for genetic material. ut not evidence that #0! carries information
*eedac+ %) True. and useful for genetic material. ut not evidence that #0! carries information
*eedac+ #) :ften cited. ut tainted y the FmostG termH this is not as "o(erful a demonstration as choice
F!G
*eedac+ &) True. and an indication that information may e "resent. ut not actually evidence that #0!
carries information
83@. !ll of the follo(ing can stimulate the activity of muscle glycogen "hos"horylase &?%&PT
!. calcium ions.
$. e"ine"hrine.
%. cyclic !4P.
&. glucagon.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &) !ffects the liver and +idney. ut not muscle.
831. 9hat is 0:T required for oxygenation of ,;
!. one heme ound "er suunit
$. iron atom in ferric valence state
%. ru"ture of at least eight salt ridges
#. oxygen "artial "ressure in excess of 5 mm ,g
&. decrease in the "ac+ing density et(een al"ha1Jeta3 chains
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) *ull oxygenation is (hen all four of the suunits have ound one oxygen molecule.
*eedac+ $) *errous state -*e 3<2. not ferric.
*eedac+ %) %hanges that facilitate coo"erativity.
*eedac+ #) The first oxygen molecule is the most difficult to ind. and then ,Is affinity for oxygen
increases (ith each additional oxygen ound.
*eedac+ &) %onformational changes facilitating coo"erativity.
833. 9hich mitochondrial en1yme requires acetyl5%o! as a sustrate;
!. %itrate synthase
$. 'uccinyl5%o! synthase
%. 'uccinic dehydrogenase
#. Pyruvate dehydrogenase
&. Isocitrate dehydrogenase
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) In the first ste" of T%! cycle acetyl %o! < oxaloacetate 5556 citrate
*eedac+ $) /equires %o!. ut not acetyl %o!.
*eedac+ %)
*eedac+ #) Produces acetyl %o!.
*eedac+ &)
838. The synthesis of dT4P from its immediate "recursor involves
!. reduction of rT4P
$. methylation of dL4P
%. a reaction cataly1ed y rionucleotide reductase
#. deamination of d%4P
&. salvage of thymidine (ith the activated sugar derivative P/PP
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) 0o such thing exce"t as a "ost5transcri"tional modification in existing /0!
*eedac+ $) Yes. the reaction cataly1ed y thymidylate synthase
*eedac+ %) 0o. /0/ acts earlier during conversion of r%#P or rL#P to d%#P or dL#P (hich eventually
"rovide the dL4P that is the immediate "recursor of dT4P.
*eedac+ #) This "roduces dL4P (hich is the immediate "recursor for dT4P synthesis
*eedac+ &) This can ha""en at a very lo( frequency. ut is not a maDor "ath(ay for "roducing dT4P
834. !llosteric control most often occurs through changes in
!. en1yme levels.
$. sustrate concentrations.
%. Mmax.
#. 7m.
&. "hos"horylationJde"hos"horylation.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) This is not allosteric control of the en1yme. &n1yme levels are determined y control of
transcri"tion. translation. andJor degradation.
*eedac+ $) !llosteric control modifys the affinity or catalytic activity of the en1yme in res"onse to levels
of s"ecific molecules. It is the change in affinity or activity that is the control.
*eedac+ %) %ould occur ut it is not the most common mode of control.
*eedac+ #) !llosteric control usually involves a change in the en1ymeIs affinity for the sustrate.
*eedac+ &) This is a covalent modification rather than an allosteric control.
835. !n anormal hemogloin -,2 (as identified (ith reduced #PG inding. 9hat is the "hysiological
consequence;
!. reduced oxygen inding to ,
$. reduced $ohr effect
%. enhanced methemogloin formation
#. increased turnover of hemogloin
&. less oxygen transfer to tissues
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) *alse. decreased #PG inding 5556 increased :3 affinity of ,
*eedac+ $) Irrelevant ecause the $ohr effect involves ,< and %:3.
*eedac+ %) 'ounds im"ressive ut see &.
*eedac+ #) 'ounds im"ressive ut see &.
*eedac+ &) decreased #PG inding 5556 increased :3 affinity of ,. so :3 is not as readily released to
the tissues.
836. 9hich is a "ositive allosteric effector of "yruvate caroxylase;
!. Glucose 65"hos"hate
$. !cetyl5%o!
%. %itrate
#. !#P
&. !TP
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $) Pyruvate caroxylase cataly1es the 1st ste" of gluconeogenesis) "yruvate < iotin5%:3 5556
oxaloacetate (here %:3 is added to iotin only (hen acetyl %o! is ound to "yruvate caroxylase.
*eedac+ %) %itrate "romotes gluconeogenesis y stimulating fructose 1.65is"hos"hatase.
*eedac+ #)
*eedac+ &)
83=. In human cells
!. the re"lication or ' "hase lasts aout > hours
$. re"lication initiates at aout 4@@@ sites "er cell called origins
%. re"lication and segregation overla" to allo( shorter division cycles
#. origins fire in grou"s of aout 1@@@ re"licons called atteries
&. re"lication is continuous on oth leading and lagging strands
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) This is a ty"ical value for a ty"ical human cell
*eedac+ $) ,uman cells activate aout 4@.@@@ origins of re"lication
*eedac+ %) This occurs in "ro+aryotes. ut not in eu+aryotes. including humans
*eedac+ #) $atteries re"resent 1@51@@ origins that fire coordinately
*eedac+ &) 0: +no(n re"lication system has continuous lagging strand synthesis.
83>. 9hat change from normal is li+ely to result from the ingestion of ethanol;
!. Increased reduction of "yruvate
$. Increased conversion of 5hydroxyutyrate to acetoacetate
%. #ecreased +etogenesis due to lac+ of acetyl5%o!
#. Increased "roduction of oxaloacetate from malate
&. Increased "roduction of dihydroxyacetone "hos"hate from glycerol "hos"hate
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) 4etaolism of ethanol y the liver increases the cytosolic concentration of 0!#, (hich
"romotes the reactions) "yruvate < 0!#, 5556 lactate < 0!#< oxaloacetate < 0!#, 5556 malate <
0!#<
*eedac+ $) &thanol metaolism increases the cytosolic 0!#, levels and (ould "romote the reverse
reaction) acetoacetate < 0!#, 5556 5hydroxyutyrate < 0!#<
*eedac+ %)
*eedac+ #) ,igh 0!#, (ould "romote the reverse reaction) :xaloacetate < 0!#, 5556 malate < 0!#<.
*eedac+ &) Increased cytosolic 0!#, (ould "romote the reverse reacion) dihydroxyacetone "hos"hate <
0!#, 5556 glycerol "hos"hate < 0!#<
83A. 4utations that affect al"ha1eta3 interface can increase the amount of dimeric hemogloin. 9hat is
the consequence of dimeric ,;
!. reduced oxygenation
$. increased #PG inding
%. increased oxygenation
#. enhanced methemogloin formation
&. heme "reci"itation
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) 'ee %
*eedac+ $) #PG cross5lin+s eta5chains in the tetramer. does not effectively interact (ith a dimer.
*eedac+ %) Boose coo"erativety and loss of #PGIs effect ma+e the dimeric , more li+e myogloin (ith
high oxygen affinity.
*eedac+ #) 'ounds im"ortant ut see %.
*eedac+ &) 'ounds im"ortant ut see %.
88@. &ach of the follo(ing is generally true aout 0I##4 &?%&PT -$!# TL&'TI:0. credit (as given for 3
of the follo(ing2
!. It is associated (ith "olydy"sia and "olyuria.
$. Insulin is not detected in serum.
%. :esity in 0I##4 is common.
#. There is a strong genetic com"onent.
&. There are antiodies against normal insulin.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) True. these are common sym"toms of diaetes.
*eedac+ $) The ans(er ex"ected (as &. ut credit (as also given for this res"onse. This is false ecause
the "ancreas retains $5cells and insulin levels are ty"ically high in oese 0I##4 "atients.
*eedac+ %) True
*eedac+ #) True
*eedac+ &) This (as the ex"ected ans(er. ut credit (as also given for $. This is false ecause 0I##4
does not involve viruses or autoimmune antiodies.
881. #irect reversal of thymine dimers using the energy otained from incident light is cataly1ed y
!. a com"lex of Lvr!. Lvr$. and Lvr%
$. "hotolyase
%. the re"airosome
#. thymidine deaminase
&. "hytochromase
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) These are en1ymes of 0ucleotide &xcision /e"air -0&/2. not "hotoreversal
*eedac+ $)
*eedac+ %) I made this u"
*eedac+ #) I made this u". thymidine doesnIt have anything to deaminate (ith.
*eedac+ &) I made this u"
883. %ataolism of 1@@ g of carohydrate. 35 g of fat. and 3@ g of "rotein yields a""roximately ho( many
%als;
!. 8@@
$. 5@@
%. =@@
#. A@@
&. 11@@
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) 'ee %
*eedac+ $) 'ee %
*eedac+ %) 1@@g car -4 %alsJg2 < 35g fat -A %alJg2 < 3@ g "rotein -4 %alJg2 P =@5 %als
*eedac+ #) 'ee %
*eedac+ &) 'ee %
888. 4ost "e"tide onds in naturally occurring "roteins)
!. "referentially ado"t a trans configuration
$. "referentially ado"t a cis configuration
%. sho( no "reference for trans or cis configurations
#. never assume a cis configuration
&. never assume a trans configuration
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) #oule ond character of the "e"tide ond is more stale in a trans configuration.
*eedac+ $) In all cis "e"tides mutual hindrance et(een neighoring side5chains is severe.
*eedac+ %)
*eedac+ #)
*eedac+ &)
884. 9hich of the follo(ing is *!B'& aout glucagon;
!. It decreases in lood as glucose increases.
$. It "romotes the rea+do(n of he"atic and muscle glycogen.
%. It "romotes gluconeogenesis in liver.
#. It "romotes li"ase activity in adi"ocytes.
&. It can stimulate adenylate cyclase.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) True. as lood glucose rises insulin levels increase and glucagon levels decrease.
*eedac+ $) *alse. glucagon does not affect muscle.
*eedac+ %) True. in order to maintain lood glucose et(een meals.
*eedac+ #) True. to "rovide fuel molecules (hen glucose is lo(.
*eedac+ &) Glucagon inding to its rece"tor activates adenylate cyclase.
885. Besch50yhan 'yndrome is associated (ith the loss of
!. xanthine oxidase
$. adenylate cyclase
%. thymidylate synthase
#. hy"oxanthine5guanine "hos"horiosyl transferase
&. dihydrofolate reductase
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
886. %yclic G4P -unli+e cyclic !4P2 causes fe( notale metaolic changes. ut cyclic G4P does
!. stimulate cyclic !4P "hos"hodiesterase-s2.
$. relax smooth muscle in vascular eds.
%. cause the release of calcium from the sarco"lasmic reticulum.
#. reverse effects of insulin.
&. stimulate "hos"hatase51.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $) 0itric oxide activates cytosolic guanylate cyclase. Increased cG4P then induces smooth
muscle relaxation.
*eedac+ %)
*eedac+ #)
*eedac+ &)
88=. %onsider the "e"tide) Gly5'er5Glu5!s"5Bys5Mal5Pro !t neutral ",. the overall charge on the "e"tide
(ill e a""roximately)
!. 58
$. 51
%. @
#. <1
&. <8
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $) 'ide chain charges are) Gly -@25'er -@25Glu -5125!s" -5125Bys -<125Mal -@25Pro-@2
*eedac+ %)
*eedac+ #)
*eedac+ &)
88>. Glycogen degradation in muscle can e increased y each of the follo(ing &?%&PT for
!. calcium ion.
$. "hos"horylated glycogen "hos"horylase +inase.
%. "hos"horylated glycogen synthase.
#. high e"ine"hrine.
&. increased cyclic !4P in the cell.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) *luxes of %a3< act as a mediator of contraction and energy use in muscle.
*eedac+ $) &"ine"hrine inds to rece"tor 5556 c!4P levels increase 5556 "hos"horylation of glycogen
"hos"horylase +inase 5556 "hos"horylation of glycogen "hos"horylase 5556 glycogen degradation
*eedac+ %) Glycogen synthase is inactive (hen "hos"horylated and thus not synthesi1ing glycogen. ut
this does not increase degradation.
*eedac+ #) 'ee $
*eedac+ &) 'ee $
88A. The staility of #0! du"lexes is increased y
!. increasing the tem"erature aove 3@ degrees %
$. changing the ", to values near =
%. adding formamide or other non5aqueous solvents
#. decreasing the concentration of salts
&. the hy"ochromic shift
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) Increasing the tem"erature decreases the staility of du"lex #0!
*eedac+ $) Yes. #0! is most stale near neutral ",s ecause this o"timi1es the formation of hydrogen
onding interactions
*eedac+ %) #0! is staili1ed y the hydro"hoic effect (hich is less im"ortant as the solvent ecomes
less "olar.
*eedac+ #) ,igher ionic strengths staili1e #0! due to shielding of the re"ulsive interactions et(een
the charged "hos"hodiester ac+ones. 'o decreasing the salt destaili1es #0!
*eedac+ &) The hy"ochromic shift is a consequence of formation of du"lexes et(een t(o single strands.
It does not influence the staility of the molecules. it is an effect of the formation of ds#0!.
84@. The term Eoxidative stressE refers to
!. the fact that oxidative "hos"horylation requires !#P -res"iratory control2.
$. the formation of oxygen free radicals ecause of the incom"lete reduction of molecular oxygen.
%. the fact that oxidative "hoso"horylation requires molecular oxygen.
#. the inaility of aeroic glycolysis to meet energy demands during strenuous exercise.
&. the uncou"ling of oxidative "hos"horylation.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $) *ree radicals can initiate harmful chain reactions. and ecause an essential "art of our
metaolism is reducing :3 to ,3: there is a constant stress on the cell to deal (ith oxygen free radicals.
*eedac+ %)
*eedac+ #)
*eedac+ &)
841. &n1ymes use (hich of the follo(ing to lo(er the energy of activation;
!. change in sustrate "olarity
$. !TP hydrolysis
%. sustrate strain
#. tem"erature variation
&. solvation of sustrate
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $) %an "rovide energy to reach activation energy.
*eedac+ %) &n1yme active sites are com"lementary to the transition states of the reacting s"ecies.
*eedac+ #) Increased tem"erature is a (ay to increase rates of reactions. ut it is not ho( en1ymes
(or+.
*eedac+ &)
843. !ll of the follo(ing statements aout the en1ymic com"lex that carries out the synthesis of !TP
during oxidative "hos"horylation are correct &?%&PT
!. It is located on the matrix side of the inner mitochondrial memrane.
$. It is inhiited y oligomycin.
%. It contains a "roton channel.
#. It can exhiit !TPase activity.
&. It can ind molecular oxygen.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) The "roton conducting *@ unit is in the inner mitochondrial memrane and the !TP
synthesi1ing *1 unit in on the matrix side.
*eedac+ $) :ligomycin inds to the *@ unit of the !TP5synthase "reventing "roton flux through the
channel to the *1 unit.
*eedac+ %) 'ee !
*eedac+ #) If the "ro"er N,<O gradient is not "resent the en1yme can hydroly1e !TP instead of
synthesi1ing it.
*eedac+ &) *alse. %ytochrome aJa8 of the electron trans"ort chain contains a heme iron that inds :3.
848. ,istones are usually
!. !cidic. and therefore "ositively charged at neutral ",
$. !cidic. and therefore negatively charged at neutral ",
%. $asic. and therefore "ositively charged at neutral ",
#. $asic. and therefore negatively charged at neutral ",
&. %lose to neutral. and therefore uncharged at neutral ",
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) 'ee %
*eedac+ $) 'ee %
*eedac+ %) $asic residues are "rotonated at neutral ",s and are therefore "ositively charged. ,istones
have a high "ro"ortion of asic residues.
*eedac+ #) 'ee %
*eedac+ &) 'ee %
844. The numer of moles of sustrate converted to "roduct "er minute "er mol of en1yme is the)
!. 7m
$. Mmax
%. turnover numer
#. a""arent 7m
&. 7mJMmax
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) 7m is the concentration of sustrate -N'O2 (hich gives half maximal velocity -1J3 Mmax2.
*eedac+ $) Mmax is the maximum velocity of "roduct formation.
*eedac+ %) %an e stated several different (ays ut is asically) amount of sustrate to "roduct "er
en1yme amount "er time.
*eedac+ #) Increase is 7m in the "resence of a com"etative inhiitor.
*eedac+ &) 'lo"e of the Bine(eaver5$ur+e "lot.
845. 9hich of the follo(ing is 0:T in the "yrimidine family;
!. thymine
$. cytosine
%. uracil
#. orotate
&. hy"oxanthine
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) This is a "yrimidine
*eedac+ $) This is a "yrimidine
*eedac+ %) This is a "yrimidine
*eedac+ #) :rotic acid is the ase that is converted to a nucleotide during "yrimidine synthesis.
*eedac+ &) ,y"oxanthine is a "urine
846. 9hich of the follo(ing statements is 0:T true; !llosteric en1ymes ...
!. sho( sigmoidal +inetics
$. are often multisuunit structures
%. are often regulated y effector molecules
#. have at least t(o s"ecific inding sites
&. suunits exhiit minimal interactions (hen the en1yme is oligomeric
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) True. 4ichaelis54enten +inetics give hy"erolic curves. allosteric +inetics give sigmoid
curves.
*eedac+ $) True. ,emogloin -although not an en1yme2 is a great exam"le of allosteric control. , is a
tetramer.
*eedac+ %) True. , oxygen affinity is affected y %:3. ,<. and #PG inding at allosteric sites.
*eedac+ #) True. at least one allosteric site and an active site.
*eedac+ &) *alse. suunits can e highly interactive (ith each other. as in ,.
84=. 9hich of the follo(ing com"ounds (ould #I/&%TBY serve as a sustrate of the en1yme that converts
rionucleotides to deoxyrionucleotides;
!. G#P
$. L4P
%. %4P
#. dT4P
&. !TP
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) /0/ acts only on rionucleoside di"hos"hates
*eedac+ $) /0/ acts only on rionucleoside di"hos"hates. this is a mono"hos"hate
*eedac+ %) /0/ acts only on rionucleoside di"hos"hates. this is a mono"hos"hate
*eedac+ #) /0/ acts only on rionucleoside di"hos"hates. this is a deoxy sugar and a mono"hos"hate
*eedac+ &) /0/ acts only on rionucleoside di"hos"hates. this is a tri"hos"hate
84>. ! noncom"etitive inhiitor (ill affect
!. 7m
$. Mmax
%. 7m and Mmax
#. the a""arent 7m
&. en1yme staility
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) Is not affected ecause the noncom"etative inhiitor does not interfere (ith the inding of
sustrate to the en1yme.
*eedac+ $) 0oncom"etative inhiition cannot e overcome y an increase in N'O. and thus Mmax is
affected.
*eedac+ %) :nly Mmax is affected. 'ee ! and $.
*eedac+ #) 7m is higher in the "resence of a com"etative inhiitor ut unaffected y a noncom"etative
inhiitor.
*eedac+ &) Vust "lain no.
84A. 9hich sustance does 0:T contriute to the ring atoms during the synthesis of "urines;
!. !s"artate
$. !rginine
%. Glycine
#. Glutamine
&. 051@5tetrahydrofolate
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) 'ee $
*eedac+ $) 'ounds trivial. ut I found this exact question on the 1AA1 oard exam that I Dust received.
so I thre( it in.
*eedac+ %) 'ee $
*eedac+ #) 'ee $
*eedac+ &) 'ee $
85@. &n1ymes cataly1e reactions commonly y
!. lo(ering the activation energy
$. activating cofactors
%. shifting the equilirium to a more favorale "osition
#. increasing the energy content of the sustrate
&. "rotecting sustrates from solvent hydrolysis
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) !ctivation energy is lo(ered through inding energy and transition state staili1ation.
*eedac+ $) 0o. many en1ymes do not have cofactors.
*eedac+ %) &n1ymes do not affect equilirium.
*eedac+ #) 0o. they lo(er the energy of activation.
*eedac+ &) Vust ecause there needs to e an &.
851. Purified rionucleotide reductase
!. ma+es more d%#P in the "resence of dTTP
$. ma+es more dG#P in the "resence of d!TP
%. ma+es less dL#P in the "resence of !TP
#. ma+es more d!#P in the "resence of dGTP
&. ma+es less dG#P in the "resence of dTTP
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) 'ee the regulation chart in lecture 3. "age 5
*eedac+ $) 'ee the regulation chart in lecture 3. "age 5
*eedac+ %) 'ee the regulation chart in lecture 3. "age 5
*eedac+ #) 'ee the regulation chart in lecture 3. "age 5
*eedac+ &) 'ee the regulation chart in lecture 3. "age 5
853. 9hat is a "ossile defect in the &hlers5#anlos syndrome;
!. defective conversion of "rocollagen to tro"ocollagen
$. failure to en1ymatically form lysinonorleucine crosslin+s
%. defective hydroxylation of "roline
#. defective disulfide ond formation in elastin
&. inactivation of inhiitor of elastase
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) In some cases an anormal "rocollagen "e"tidase does not remove the "ro"e"tides.
*eedac+ $) This is Bathyrism
*eedac+ %) This is 'curvy
*eedac+ #) Im"ressive sounding. ut no.
*eedac+ &) !l"ha15antitry"sin deficiency can lead to em"hysema due to destruction of alveolar (alls y
elastase.
858. 9hich of the follo(ing is a general feature of oth #0! and /0!;
!. Their secondary structures can include G5% ase "airs
$. They interact (ith histones to form nucleosomes
%. they are usually found as helices formed from t(o se"arate chains
#. Phos"hodiester onds lin+ the 5Q and 3Q hydroxyls of adDacent sugars
&. They are stale in high ", solutions
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $) 0ucleosomes contain #0!. not /0!
*eedac+ %) ds/0! involving t(o se"arate strands does form and can e found in nature. ut is not the
usual case for /0! as it is for #0!
*eedac+ #) $oth /0! and #0! contain "hos"hodiester ac+ones (ith 5I and 8I lin+ages. not 3I.
*eedac+ &) The secondary structure of #0! is unstale at high ",. and oth the secondary and "rimary
-"hos"hodiester ac+one2 structures of /0! are unstale at high ",
854. The histidine residue (ithin the catalytic triad in chymotry"sin "artici"ates in the follo(ing)
!. facilitates the "rotonation of 'er as the initial event in catalysis
$. serves as a "roton donor and acce"tor
%. serves only as a "roton donor
#. forms a salt ridge to the side chain caroxylate of the sustrate
&. hydrogen onds to the caronyl of the laile ond in the sustrate
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) The initial event is the de"rotonation of serine.
*eedac+ $) True due to its (ea+ly asic character ,is can acce"t and donate ,< at "hysiological ",. Its
imida1ole ring can quite easily accommodate either state.
*eedac+ %) 'ee $.
*eedac+ #)
*eedac+ &)
855. Production of thymidylate in human cells can e inhiited y administering
!. methotrexate
$. folic acid
%. acyclovir
#. leucovorin
&. dL4P
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) This loc+s #,*/ activity. "reventing rene(al of the required activated folate cofactor for
thymidylate synthase
*eedac+ $) *olate is required for thymidylate synthase. it is not an antagonist
*eedac+ %) This is a chain5terminator if "hos"horylated and therefore loc+s #0! re"lication. ut only in
cells infected (ith her"esviruses -and therefore contain a thymidylate +inase that (ill (or+ on this
analog2. and not y loc+ing thymidylate synthesis.
*eedac+ #) Beucovorin is an activated folate that rescues cells from the effects of #,*/ inhiitorsH it is
an activator of thymidylate synthesis
*eedac+ &) dL4P is the sustrate for thymidylate synthase and so (ould not e ex"ected to loc+ dT4P
synthesisH in fact. Dust the o""osite if it could get into cells.
856. Treatment of hy"eruricemia. or gout. involves administering allo"urinol (hich
!. "revents isomeri1ation of uric acid from the +eto to the insolule enol form
$. com"etes (ith urate for secretion y the +idneys
%. inhiits xanthine oxidase
#. decreases the serum concentration of xanthine
&. inhiits ,GP/Tase
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) Yes. this decreases the formation of uric acid.
*eedac+ #)
*eedac+ &)
85=. 9hich "air of oligonucleotide "rimers (ould am"lify the follo(ing EtargetE sequence in a P%/
ex"eriment) 5Q5GT!T!%G!%%...target...T!G%!T!G!%58Q
!. 5Q5T!G%!T!G!% and 5Q5GGT%GT!T!%
$. 5Q5GT!T!%G!%% and 5Q5T!G%!T!G!%
%. 5Q5GGT%GT!T!% and 5Q5GT%T!TG%T!
#. 5Q5GT!T!%G!%% and 5Q5GT%T!TG%T!
&. 5Q5GT!T!%G!%% and 8Q5T!G%!T!G!%
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) $oth "rimers "oint a(ay from the target.
*eedac+ $) The first "rimer is correct. ut the second anneals to the same strand and "oints a(ay from
the target.
*eedac+ %) The second "rimer is correct. ut the first anneals to the same strand and "oints a(ay from
the target.
*eedac+ #) The sequence at the 5I end of the given strand and the sequence at the 5I end of the
com"lementary strand.
*eedac+ &) The first "rimer is correct. ut the second anneals to the same strand and "oints a(ay from
the target.
85>. If you (ere to reanneal 1 microgram of denatured yeast #0! and 1 microgram of denatured human
#0! se"arately in equal total volumes under equal solution conditions. you should ex"ect
!. the yeast #0! to decrease in total ultraviolet light asorance faster than the human #0!
$. the human #0! to increase in total ultraviolet light asorance slo(er than the yeast #0!
%. the yeast #0! sam"le to have fe(er co"ies of any given sequence since the genome is smaller
#. the human #0! sam"le to contain more /0! ecause the human genome has more genes
&. oth sam"les to anneal at the same rate ecause the concentration of #0! is the same
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) Yes. yeast #0! is less com"lex than human #0!. so any given sequence is "resent more
times in the same total mass of #0! and (ill e higher in concentration in equivalent sam"les. and (ill
therefore anneal more quic+ly. *ormation of doule stranded helices leads to a lo(ering of LM asorance
-the hy"ochromic shift2 (hich (ill therefore occur faster (ith the yeast #0!.
*eedac+ $) 0o. annealing (ill e slo(er (ith the human #0! -see ans(er !2. ut during annealing LM
asorance is decreased not increased.
*eedac+ %) The genome is smaller. ut this means that an equivalent mass of #0! (ill have more co"ies
of the yeast genome.
*eedac+ #) It is true that the human #0! has more genes. ut the #0! sam"les shouldnIt have /0! in
them at all.
*eedac+ &) This (ould e true if oth sam"les had the same com"lexity. ut they donIt. 'ee ans(er !.
85A. You have "roed a 'outhern lot (ith a laeled #0! "roe ut find that you get hyridi1ation to too
many EtargetE sequences. You correctly infer that you are getting hyridi1ation to sequences similar to.
ut not identical to. the intended target. ,o( (ould you increase the s"ecificity of the hyridi1ation;
!. #ecrease the hyridi1ation time
$. Increase the hyridi1ation tem"erature
%. #ecrease the amount of organic solvent in the hyridi1ation solution
#. Increase the concentration of salt in the hyridi1ation solution
&. #ecrease the stringency of the hyridi1ation solution
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) 0o. this (ill reduce the signal from oth the correct and incorrect targets.
*eedac+ $) Yes. this (ill increase the stringency and only allo( correctly matched du"lexes to remain.
*eedac+ %) 0o. the o""osite (ould hel" to increase the stringency
*eedac+ #) 0o. this (ould staili1e du"lexes. (hich (ould reduce the stringency
*eedac+ &) 0o. increasing the stringency is called for.
86@. $acterial fertility factors
!. are transferred from one cell to another. leaving the original host cured of the factor
$. are limited to transfers et(een cells of the same s"ecies
%. are toxic to "athogenic acteria and are eing develo"ed as antiiotics
#. are "lasmids ca"ale of conferring resistance to multi"le antiiotics simultaneously
&. induce acteria to undergo meiosis and s"ore formation
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) They are transferred. ut they are co"ied at the same time leaving oth cells FinfectedG
*eedac+ $) 0o. s"ecies oundaries can e crossed y these elements
*eedac+ %) 'ee #
*eedac+ #) #isturing ut true
*eedac+ &) 9ell. theyIre called fertility factors...ut no. acteria donIt do meiosis
861. The synthesis of dTTP. and therefore also #0! re"lication. is inhiited clinically y administering a
"recursor of a suicide sustrate of thymidylate synthase called)
!. methotrexate
$. 55fluorouridine
%. acyclovir
#. !llo"urinol
&. $oth a and are correct
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) 0o. this (or+s. ut acts y "reventing cycling of folate forms. not y targeting thymidylate
synthase.
*eedac+ %) 0o. this is a chain terminator effective against cells infected (ith her"esviruses.
*eedac+ #) 0o. this is an inhiitor of xanthine oxidase
*eedac+ &) 0o. ! is incorrect.
863. ! du"lex #0! molecule
!. is aout 8@ nm in diameter and has aout 6 ase "airs "er helical turn
$. is aout 1@ nm in diameter and has aout 1@ ase "airs "er helical turn
%. is aout 3 nm in diameter and has aout 1@ ase "airs "er helical turn
#. is aout 1@ nm in diameter and has aout 16 ase "airs "er helical turn
&. is aout 3 nm in diameter and has aout 16 ase "airs "er helical turn
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) 'ee %
*eedac+ $) 'ee %
*eedac+ %) Vust chec+ing for a sense of scale. ,ad a $iochemistry Ph.#. candidate fail to ans(er this
question once and havenIt quite gotten over it.
*eedac+ #) 'ee %
*eedac+ &) 'ee %
868. Ty"e II to"oisomerase inhiitors that are used clinically as antiiotics include
!. leucovorin
$. MP16
%. 55fluorocytosine
#. fluoroquinolones
&. $oth and c are correct
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) 0o. this a form of folate used to rescue "atients from the harmful effects of methotrexate
treatment.
*eedac+ $) 0o. this is a ty"e II to"o inhiitor. ut only in eu+aryotes.
*eedac+ %) 0o. this is an antiiotic. ut it targets thymidylate synthase. not to"o
*eedac+ &) 0o. neither is correct.
864. 4utations caused y one of the follo(ing agents almost al(ays inactivate genes s"ecifying "rotein
it;
!. LM light
$. cis5"latin
%. 55romouracil
#. 4ethyl5methane sulfonic acid -44'2
&. en1oNaO"yrene
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) *orms "yrimidine dimers. not frameshiftsH see &
*eedac+ $) crosslin+er. not a frameshifterH see &
*eedac+ %) mismatches due to tautomer shift staili1ation. not frameshiftsH see &
*eedac+ #) mismatches due to al+ylation of ases. not frameshiftsH see &
*eedac+ &) an intercalater and notorious frameshifter. this is much (orse for :/*s -"roteins2 than
structural /0!s.
865. !n inhiitor of telomerase (ould e ex"ected to
!. cause telomeres to get shorter
$. cause cells to age faster
%. "romote gro(th of tumors
#. inhiit gro(th of firolasts
&. "romote immortali1ation of cultured cells
'ho( ans(er
%orrect !ns(er) !
*eedac+ !) Yes. a telomerase inhiitor (ould "revent telomere elongation.
*eedac+ $) 0o. the correlation et(een age and telomere length has not een sho(n to e causal.
*eedac+ %) 0o. loss of telomerase should hel" to "revent tumor gro(th. although this is still eing
tested.
*eedac+ #) Yes. cells need to elongate their telomeres to gro( indefinitely
*eedac+ &) 0o. immortali1ation requires activation of telomerase. not inhiition.
866. cis5"latin
!. loc+s synthesis of folate and therefore "revents #0! re"lication
$. "romotes soluili1tion of urate and therefore "revents attac+s of gout
%. is an intercalating agent and therefore affects "rotein coding regions more than structural /0!s
#. causes thymine dimers and therefore can e used to target tumors defective in mismatch re"air
&. is a #0! crosslin+er used clinically to target ra"idly gro(ing tumors
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) 0o. this is a crosslin+er used to selectively +ill ra"idly gro(ing cells
*eedac+ $) 0o. this is a crosslin+er used to selectively +ill ra"idly gro(ing cells
*eedac+ %) 0o. this is a crosslin+er used to selectively +ill ra"idly gro(ing cells
*eedac+ #) 0o. this is a crosslin+er used to selectively +ill ra"idly gro(ing cells
*eedac+ &)
86=. 9hich amino acid can commonly functions as an acid and ase in catalysis;
!. 'er
$. Tyr
%. Ile
#. ,is
&. Bys
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #) ,istidine has an imida1ole ring that accommodates s(itches et(een "rotonated and
un"rotonated states. and its "7a is close to "hysiological ",.
*eedac+ &)
86>. Xymogens are commonly activated y)
!. !ddition of "roteoli"id
$. !ddition of glycoli"id
%. Proteolysis
#. Phos"horylation
&. !#P5riosylation
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) Xymogens are inactive en1yme "recursors that are commonly activated y cleavage of
"e"tide onds.
*eedac+ #)
*eedac+ &)
86A. 9hich is 0:T true of the staility of "roteins that are "redominantly al"ha helical in structure;
!. Pac+ing of al"ha helical segments
$. ,ydrogen onding et(een ac+one amides of one helix and caronyl oxygens of a second helix
%. ,ydrogen onding et(een side chains of different helices
#. Pac+ing of hydro"hoic residues in the "rotein interior
&. 'taili1ing interactions (ithin reverse turns connecting t(o helices
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $) ,ydrogen onding occurs et(een ac+one amides and caronyl carons that are 4
residues a"art (ithin the helix.
*eedac+ %) The side chains are staggered on the surface of the helix and can interact (ith side chains of
other helices.
*eedac+ #)
*eedac+ &)
8=@. 'ic+le cell anemia results from)
!. 'taility of oxy5hemogloin in venous lood
$. /educed #PG inding
%. Bac+ of heme inding to hemogloin chains
#. 4yogloin "reci"itation
&. Polymeri1ation of deoxy5hemogloin
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $) *etal , has a lo(er affinity for #PG. and thus a higher affinity for oxygen.
*eedac+ %)
*eedac+ #)
*eedac+ &) 'ustitution of glutamate y valine "laces a non"olar residue on the outside of ,'. (hich
inds to a stic+y "atch that is ex"osed on another deoxy ,.
8=1. ,y"oglycemia can results from a deficiency of each of the follo(ing &?%&PT
!. fructose51.65is"hos"hatase
$. glucose565"hos"hatase
%. "hos"hoenol"yruvate caroxy+inase
#. "yruvate caroxylase
&. "yruvate dehydrogenase
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) Gluconeogenesis
*eedac+ $) Gluconeogenesis
*eedac+ %) Gluconeogenesis
*eedac+ #) Gluconeogenesis
*eedac+ &) !ll of the other en1ymes listed are needed for gluconeogenesis. Pyruvate dehydrogenase is
needed to transfer from glycolysis to T%! cycle.
8=3. The source of most ammonia excreted into the urine from the +idneys of most verterate animals is
!. alanine
$. as"aragine
%. glutamic acid
#. glutamine
&. arginine
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #) Glutamine from all tissues is trans"orted to the liver (here it is hydroly1ed to glutamate and
ammonia. and urea is then synthesi1ed.
*eedac+ &)
8=8. ! deficiency of glucose565"hos"hate dehydrogenase most often a""ears clinically as
!. hy"oglycemia
$. hy"eruricemia
%. hy"erglycemia
#. hemolytic anemia
&. hy"oricemia
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #) /$%Is are highly affected ecause their only means of generating 0!#P, is the ,4P
"ath(ay. for (hich glucose565"hos"hate is needed.
*eedac+ &)
8=4. Insulin causes each of the follo(ing changes &?%&PT
!. !n increase in tyrosine +inase activity
$. ! decrease in gluconeogenesis
%. !n increase in triglyceride rea+do(n to fatty acids
#. ! relative decrease in circulating glucose
&. !n increase in glycogen synthesis
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) The insulin rece"torIs cytosolic domain is a tyrosine +inase
*eedac+ $) Glucose levels are high. so the ody does not need to synthesi1e glucose.
*eedac+ %) 0o. glucose is high an can e used for an energy source and excess is coverted to fatty acids
for storage.
*eedac+ #) #ue to the u"ta+e of glucose into cells.
*eedac+ &) *or storage of excess glucose.
8=5. The Ecommitted ste"E of glycolysis occurs at (hich en1yme;
!. Glucose 65"hos"hate
$. P*751
%. Gluco+inase
#. *ructose 1.65is"hos"hate
&. ,exo+inase
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $) Vust memori1e it.
*eedac+ %)
*eedac+ #)
*eedac+ &)
8=6. The reaction (hich requires a continuous su""ly of 0!#< for glycolysis is
!. Isomeri1ation of glucose 65"hos"hate
$. Phos"horylation of glucose
%. :xidation of glyceraldehyde 85"hos"hate
#. %leavage of fructose 1.65is"hos"hate
&. Phos"horylation of fructose 65"hos"hate
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) Glyceraldehyde585"hos"hate is oxidi1ed and 0!#< is reduced.
*eedac+ #)
*eedac+ &)
8==. The reaction (hich is inhiited y citrate is
!. :xidation of glyceraldehyde 85"hos"hate
$. Phos"horylation of fructose 65"hos"hate
%. %leavage of fructose 1.65is"hos"hate
#. Isomeri1ation of glucose 65"hos"hate
&. Phos"horylation of glucose
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $) Phos"hofructo+inase is the en1yme for the committed ste". and thus is highly regulated.
Inhiitors) !TP. citrate. 'timulators) !4P. fructose53.65is"hos"hate.
*eedac+ %)
*eedac+ #)
*eedac+ &)
8=>. !n immediate sustrate used y the en1yme glycogen synthase is
!. Glucose
$. Glucose565"hos"hate
%. Glucose515"hos"hate
#. L4P5glucose
&. L#P5glucose
'ho( ans(er
%orrect !ns(er) &
*eedac+ !) 'ee &
*eedac+ $) 'ee &
*eedac+ %) 'ee &
*eedac+ #) 'ee &
*eedac+ &) Glucose 5556 glucose565"hos"hate 5556 glucose515"hos"hate 5556 L#P5glucose -glycogen
synthase2 5556 glycogen
8=A. 9hich of the follo(ing is *!B'& aout oxidative "hos"horylation -ox5"hos2 occurring in intact
mitochondria;
!. :x5"hos (ill sto" (hen !#P is de"leted
$. :x5"hos requires that "rotons e "um"ed out of the mitochondria matrix.
%. !TP synthesis ta+es "lace as "rotons enter the mitochondrial matrix through a s"ecific channel.
#. The addition of 3.45dinitro"henol (ill aolish electron trans"ort.
&. The addition of cyanide (ill inhiit electron trans"ort
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) True. This is res"iratory control.
*eedac+ $) &lectron trans"ort "um"s ,< from the matrix to the intermemrane s"ace and !TP is
synthesi1ed as "rotons move in the o""osite direction.
*eedac+ %) The !TP synthase has a *@ suunit that is a channel and a *1 suunit that has en1ymatic
activity.
*eedac+ #) *alse. 3.45dinitro"henol is an uncou"ler. &lectron trans"ort still "um"s ,< ut the
dinitro"henol carries the ,< ac+ into the matrix. y"assing the !TP synthase.
*eedac+ &) %yanide com"lexes (ith the ferric form of cytochrome oxidase. and %: com"lexes (ith the
ferrous form.
8>@. 9hich of the follo(ing is *!B'& aout gluconeogenesis in liver;
!. &n1ymes from the mitochondria matrix and the cyto"lasm are required.
$. This anaolic "ath(ays only occurs during "rolonged starvation.
%. This "rocess does not occur in s+eletal muscle.
#. This "rocess is indirectly stimulated y increased glucagon.
&. *atty acid oxidation su""lies energy for this "rocess.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) Pyruvate caroxylase 5 mitochondria glucose565"hos"hatase 5 &/ !ll other en1ymes needed
for gluconeogenesis 5 cytosol
*eedac+ $) *alse. It is critical during "rolonged starvation. ut it can "lay a "art in maintaining lood
glucose even et(een meals.
*eedac+ %) Gluconeogenesis occurs almost entirely in liver and +idney cells.
*eedac+ #) True. Glucagon causes the release of fatty acids (hich are converted to acetyl %o! and
increase 0!#, levels. Increased acetyl %o! stimulates "yruvate caroxylase and increased 0!#, levels
inhiit "yruvate dehydrogenase.
*eedac+ &) 'ee #.
8>1. 9hich of the follo(ing aout "yruvate dehydrogenase -P#,2 is *!B'&;
!. This en1yme is in the mitochondrial matrix.
$. %aron dioxide is a "roduct of this reaction.
%. !cetyl %o! and 0!#, oth stimulate P#,
#. '"ecific "hos"horylation of P#, decreases its catalytic activity
&. ! "roduct of the reaction cataly1ed y P#, is !cetyl %o!.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $) "yruvate < %o! < 0!#< 5556 acetyl %o! < %:3 < 0!#,
*eedac+ %) !TP. acetyl %o!. and 0!#, all inhiit "yruvate dehydrogenase.
*eedac+ #) True. ,igh levels of !TP cause the "hos"horylation.
*eedac+ &) 'ee $
8>3. The maDor immediate source of urea is
!. The hydrolysis of glutamine y glutaminase
$. The oxidative deamination of glutamic acid y glutamate dehydrogenase.
%. The oxidative deamination of amino acids y +idney #5amino acid oxidase.
#. The cleavage of arginine y arginase.
&. The hydrolysis of as"aragine y as"araginase.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) 0itrogen is trans"orted from the tissues to the liver as glutamine. and ammonia is released
(hen glutaminase hydroly1es glutamine. 0ot technically "art of the urea cycle.
*eedac+ $) 0ot "art of the urea cycle.
*eedac+ %) 0ot "art of the urea cycle.
*eedac+ #) The final ste" of the urea cycle is arginine 5556 urea < ornithine
*eedac+ &) !s"arginase removes 0,8 from as"aragine. It is not "art of the urea cycle.
8>8. !ll of the follo(ing are true aout insulin &?%&PT for
!. It contains t(o "e"tide chains.
$. It increases in serum immediately after a carohydrate rich meal.
%. It "romotes triglyceride synthesis.
#. It "romotes glycogen synthesis.
&. It "romotes gluconeogenesis
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &) Gluconeogenesis maintains lood glucose levels et(een carohydrate inta+es. (hile Insulin
release is stimulated y the inta+e of carohydrates.
8>4. 9hich of the follo(ing is the est descri"tion of lactose intolerance;
!. The genetic deficiency of galactose515Pi5uridyl transferase.
$. The genetic deficiency of lactase
%. The genetic deficiency of lacto+inase
#. The genetic deficiency of fructo+inase.
&. The de"letion of !TP in he"atocytes.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) %lassical galactosemia
*eedac+ $) The undigested lactose is metaoli1ed y colonic acteria "roducing gas and an osmotic
gradient moves fluid into the intestine "roducing diarrhea.
*eedac+ %) 0ever heard of this en1yme
*eedac+ #) &ssential fructosemia
*eedac+ &) 0o (ay
8>5. 0I##4 -ty"e 32 has each of the follo(ing characteristics -sym"toms2 &?%&PT for
!. ,y"erglycemia
$. :esity
%. 0ear normal insulin in serum
#. 7etosis
&. Polyuria
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) Ty"es 1 and 3
*eedac+ $) Ty"e 3
*eedac+ %) Ty"e 3
*eedac+ #) Ty"e 1
*eedac+ &) Ty"es 1 and 3
8>6. 9hich statement aout reactions cataly1ed y transaminases is *!B'&;
!. The equilirium constants are aout 1.@.
$. The reaction involves a 'chiff ase intermediate.
%. Pyridoxal "hos"hate is covalently ount to the transaminase en1yme.
#. !mmonia is lierated during the reaction
&. These reactions are im"ortant for the iosynthesis of some amino acids.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) This allo(s the reaction to function in oth amino acid degradation and synthesis.
*eedac+ $)
*eedac+ %) Pyridoxyl "hos"hate -a derivative of vitamin $62 is a coen1yme for aminotransferases.
*eedac+ #) *alse. The amino grou" is transfered from an amino acid to an al"ha5+eto acid.
*eedac+ &) 'ee !
8>=. The synthesis of caramoyl "hos"hate is regulated most directly y
!. Lrea
$. Glutamine
%. 05acetyl glutamate
#. !s"aragine
&. :rnithine
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) 0!G stimulates caromyl "hos"hate synthase I.
*eedac+ #)
*eedac+ &)
8>>. 9hich of the follo(ing statements is T/L& aout the condition of fructosuria
!. %an e lethal in ne(orns if untreated.
$. /eflects the genetic asence of fructo+inase.
%. /esults in de"letion of !TP in he"atocytes
#. /eflects the asence of fructase
&. /esults in hy"oglycemia
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) *ructose intolerance. not fructosuria. can e lethal. (hich is the genetic deficiency of aldolase
$.
*eedac+ $) This is a enign. asym"tomatic condition.
*eedac+ %)
*eedac+ #) 0ever heard of this en1yme
*eedac+ &) !ssociated (ith fructose intolerance.
8>A. &ach of the follo(ing can stimulate the activity of glycogen "hos"horylase in muscle &?%&PT
!. %alcium ions
$. &"ine"hrine
%. %yclic !4P
#. Glucagon
&. !ctive "hos"horylase +inase
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #) Glucagon does not affect muscle.
*eedac+ &)
8A@. E/es"iratory controlE over oxidative "hos"horylation reflects that electron flo( and !TP synthesis
sto"s (hen (hich com"ound is asent;
!. !TP
$. !#P
%. 0!#,
#. :xygen
&. *!#,
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $) &lectrons go not ty"ically flo( through electron trans"ort unless !#P is simultaneously
"hos"horylated to !TP.
*eedac+ %) 0!#, and oxygen are required for oxidative "hos"horylation. ut res"ritory control is the
need for !#P.
*eedac+ #) 'ee %
*eedac+ &)
8A1. &ach of the follo(ing is an ex"ected metaolic state after three days of starvation &?%&PT
!. The ratio of glucagon to insulin is higher than in the asor"tive state
$. *atty acids are released from adi"ose tissue
%. Gluconeogenesis ta+es "lace in liver
#. $rain uses +etones alone as an energy source
&. Biver and muscle use fatty acids as an energy source
'ho( ans(er
%orrect !ns(er) #
*eedac+ !) Glucagon increases stimulating gluconeogenesis and fatty acid release from adi"ocytes.
*eedac+ $) 'ee !
*eedac+ %) 'ee !
*eedac+ #) #uring "rolonged starvation some of the rainIs de"endence on glucose shifts to +etone
odies. ut the rain never loses its need for glucose.
*eedac+ &)
8A3. &ach of the follo(ing statements aout the hexose mono"hos"hate "ath(ay is correct &?%&PT
!. It "rovides for the synthesis of 0!#P,
$. It neither requires or generates !TP
%. It allo(s fats to e converted into glucose
#. It ta+es "lace in the cyto"lasm
&. It "rovides for the synthesis of riose from glucose
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %) *alse. ,4P "ath(ay "rovides 0!#P, needed for fatty acid synthesis.
*eedac+ #)
*eedac+ &)
8A8. The chemiosmotic theory of oxidative "hos"horylation states each of the follo(ing &?%&PT
!. :xidation and the "hos"horylation of !#P are cou"led y a "roton gradient
$. Protons are "um"ed from the matrix during electron trans"ort
%. 4olecular oxygen is reduced during oxidative "hos"horylation
#. ! "rotonmotive force drives !TP synthesis
&. The matrix side of the memrane develo"s a lo(er ", relative to the cyto"lasm side of the memrane
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %) It is reduced to (ater.
*eedac+ #) ,< -"rotons2 gradient driving the movement "rotons from the cytosolic to matrix side
through the !TP synthase.
*eedac+ &) *alse. ,< is "um"ed from the matrix to the intermemrane s"ace. so the ", in the
intermemrane s"ace is lo(er.
8A4. 9hich of the follo(ing en1ymes is B&'' !%TIM& (hen in a "hos"horylated state;
!. Glycogen "hos"hrylase
$. Triglyceride li"ase
%. Pyruvate +inase
#. Gluco+inase
&. Glycogen "hos"horylase +inase
'ho( ans(er
%orrect !ns(er) %
*eedac+ !) Increased glucagon induces "hos"horylation of glycogen "hos"horylase -stimulating2 and
"hos"horylation of glycogen synthase -inhiiting2.
*eedac+ $) Glucagon increases c!4P in adi"ocytes (hich activates the li"ase. Glucagon also induces
"hos"horylation of acetyl %o! caroxylase decreasing synthesis of fatty acids.
*eedac+ %) Glucagon induces the "hos"horylation of "yruvate +inase (hich inhiits glycolysis.
*eedac+ #) Gluco+inase activity is under transcri"tional control. 'ynthesis of gluco+inase is decreased
(hen glucagon is high.
*eedac+ &) Glucagon induced "hos"horylation increases its activity.
8A5. Bactate dehydrogenase -B#,2 cataly1ed the reversile reduction of "yruvate)
Pyruvate < 0!#, < ,<55556 Bactate < 0!#<
,o( exergonic is this reaction in the direction (ritten given the follo(ing &@Q for the half reactions; -Lse a
*araday P 38.@ %alJmol 7o2
-12 Pyruvate < 3 ,< < 3e5 5556 Bactate 5@.3@
-32 0!#, < ,< < 3e5 5556 0!#, 5@.8@
!. 5@.5
$. 53.8
%. 54.6
#. <@.5
&. <4.6
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
8A6. 9hich of the follo(ing is a *!B'& statement aout the metaolic "rocess of glycolysis;
!. Ta+es "lace in the cytosol of all mammalian cells.
$. Glycolysis itself only "rovides aout 3@K of the energy otained from glucose.
%. 4ay occur aeroically or anaeroically.
#. This "rocess converts a six caron sustrate into "yruvate.
&. !ll reactions of glycolysis are reversed during gluconeogenesis
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $) The remaining >@K is otained through T%! cycle and electron trans"ort.
*eedac+ %) !eroically the end"roduct is "yruvate !naeroically the end"roduct is lactate.
*eedac+ #) 'ee %
*eedac+ &) 0o. the three irreversile reactions of glycolysis are carried out in the reverse direction y
unique en1ymes..
8A=. T(o en1ymes required for gluconeogenesis are
!. Gluco+inase and hexo+inase
$. *ructose51.65is"hos"hatase and "yruvate caroxy+inase
%. Pyruvate +inase and glucose565"hos"hatase
#. !ldolase and +etolase
&. Phos"hofructo+inase and "yruvate +inase
'ho( ans(er
%orrect !ns(er) $
*eedac+ !) Isoen1ymes involved in glycolysis
*eedac+ $)
*eedac+ %) "yruvate +inase 55glycolysis glucose565"hos"hatase 55gluconeogenesis
*eedac+ #) !ldolase 55glycolysis 7etolase55never heard of it
*eedac+ &) glycolysis
8A>. 9hich of the follo(ing is com"lementary to the #0! sequence 5Q5%%!TT!G!%%;
!. 5Q5GGT!!T%TGG
$. 5Q5%%!TT!G!%%
%. 5Q5%%!G!TT!%%
#. 5Q5GGT%T!!TGG
&. 5Q5G%%GGT!%%T
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
8AA. !denylate cyclase from all tissues is
!. stimulated y glucagon.
$. stimulated y nore"ine"hrine.
%. intrinsic to the "lasma memrane.
#. found in the cytosol.
&. found in the mitochondrial matrix.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4@@. 9hich is li+eliest to have its structure altered y an ''$ -single5strand inding "rotein2;
!. doule5stranded #0!
$. single5stranded #0!
%. doule5stranded /0!
#. single5stranded /0!
&. an /0!)#0! hyrid
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4@1. %yclic !4P causes metaolic effects in tissues y
!. eing converted to !4P.
$. inhiiting "rotein "hos"hatase.
%. stimulating "rotein +inases.
#. inding to the allosteric site on "hos"horylase.
&. inhiiting tyrosine +inase.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4@3. The E,ershey5%haseE ex"eriment
!. "roved that only #0! can carry genetic information
$. "roved that "roteins never carry heritale genetic information
%. "rovided the ac+dro" for the later. influential. EPulse5%haseE ex"eriment
#. sho(ed that acteria can otain heritale information from dead cells
&. sho(ed that acterio"hages inDected mostly #0! into their target cells
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4@8. The most common genetic defect in humans is seen in
!. , -'ic+le cell anemia2.
$. glucose565"hos"hate dehydrogenase.
%. liver glucose565"hos"hatase -Mon Gier+eQs disease2.
#. muscle glycogen "hos"horylase -4c!rdleQs disease2.
&. muscle "hos"hofructo+inase.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4@4. You could encourage a sam"le of du"lex #0! to denature y
!. "lacing the sam"le at A@ degrees %.
$. increasing the ", to =
%. raising the concentration of salt
#. decreasing the concentration of formamide
&. increasing the melting tem"erature
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4@5. 9hich of the follo(ing is a *!B'& statement aout the "rocess of oxidative "hos"horylation;
!. It requires !#P.
$. It requires a continuous su""ly of oxygen.
%. The synthesis of !TP can e uncou"led from electron trans"ort y 3.45dinitro"henol.
#. It requires 0!#P, and 0!#, to su""ly reducing equivalents.
&. It ta+es "lace in the inner mitochondrial memrane.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4@6. !llo"urinol ameliorates the sym"toms of gout y inhiiting (hich en1yme;
!. xanthine oxidase
$. #0! "olymerase
%. Thymidine +inase
#. ,GP/Tase
&. /0! "olymerase
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4@=. Lntreated maternal diaetes during "regnancy is generally associated (ith all of the follo(ing
&?%&PT *:/
!. lo( infant irth (eight
$. maternal hy"erglycemia
%. infant hy"oglycemia at irth
#. cesarean section delivery
&. aove normal fetal insulin
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4@>. 9hich du"lex #0! -only one strand is sho(n2 (ould melt at the highest tem"erature;
!. !!TT!G%G%!!T
$. G%G%!TT!G%G%
%. G%!TT!!!TG%G
#. G!G!G!G!G!G!
&. %T%T%T%T%T%T
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4@A. %yanide is lethal ecause it
!. com"lexes to the iron of the heme in cytochrome oxidase.
$. inhiits !TP5!#P translocase.
%. com"lexes to the iron of the heme of methemogloin.
#. Euncou"lesE oxidative "hos"horylation.
&. com"lexes to uiquinone.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
41@. #efects in adenosine deaminase cause loc+age of the function of (hich en1yme. leading to (hich
disease;
!. Thymidine synthase and ,0P%%
$. ,GP/Tase and Gout
%. #0! "olymerase and %ancer
#. /0/ and '%I#
&. Thymidylate +inase and ,er"es
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
411. Liquinone -%o5T2 is unique ecause it is
!. the only carrier of single electrons.
$. the only electron carrier solule in the inner mitochondrial memrane.
%. the only electron carrier directly inhiited y cyanide.
#. the only (ater solule electron carrier.
&. the only carrier of t(o electrons.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
413. /0! is different from #0!. ecause /0!
!. is destaili1ed at high concentrations of salt
$. has thymine ut no uracil
%. is found in the ! form (hen it is a du"lex
#. has no 3Q hydroxyl
&. is stale in strongly al+aline solutions
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
418. *ollo(ing an overnight fast. during minutes after a meal of syru" and "anca+es. serum
!. insulin and glucagon increase.
$. insulin increases and glucagon decreases.
%. insulin decreases and glucagon increases.
#. insulin increases and glucagon remains constant.
&. insulin remains constant and glucagon increases.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
414. *luorocytosine is useful as an antimicroial ecause
!. it is converted to *5dL4P (hich is a suicide inhiitor of thymidylate synthase
$. the thymidylate synthase in human cells is not affected y *5dL4P
%. acteria and fungi can convert the ase to a nucleotide ut human cells canQt
#. ! and % are oth true. ut not $
&. !. $. and % are all true
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
415. 9hich of the follo(ing is *!B'& aout the en1yme "hos"hofructo+inase53 -P*7532;
!. This en1yme is in the cell cytosol.
$. This is a ifunctional en1yme (hich can have either +inase or "hos"hatase activity.
%. The "roduct of this en1yme can alter the rate of glycolysis.
#. This en1yme cataly1es the committed ste" of glycolysis.
&. *ructose565"hos"hate is a sustrate for this en1yme.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
416. Besch50yhan syndrome
!. is caused y a lac+ of hy"oxanthine5guanine "hos"horiosyl transferase
$. is associated (ith severe comined immune deficiency -'%I#2
%. is "artially corrected y factors that increase the level of urate
#. is treated (ith methotrexate
&. is associated (ith increased rates of synthesis of "yrimidines
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
41=. ! "erson (ith lactose intolerance li+ely has diminished activity of
!. lactase.
$. fructo+inase.
%. aldolase5$.
#. galacto+inase.
&. "hos"hofructo+inase.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
41>. !ssuming >5mers are an adequate length for "riming a P%/ am"lification. (hich "rimers (ill am"lify
the target elo( in a P%/; 5Q5G!%!T%!G5target5%GT!!G%T
!. 5Q5G!%!T%!G and 5Q5%GT!!G%T
$. 5Q5G!%!T%!G and 5Q5G%!TT%G!
%. 5Q5%TGT!GT% and 5Q5G%!TT%G!
#. 5Q5G!%!T%!G and 5Q5!G%TT!%G
&. There is not enough information to ans(er this question
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
41A. 0ucleosomes
!. are made of histones and aout =3 " of #0!
$. are disru"ted during the formation of the 8@ nm fier
%. contain 3 co"ies each of ,3!. ,3$. ,8. and ,4
#. cover aout =@K of the #0! in a human cell
&. contain 3 co"ies each of ,1. ,3. ,8. and ,4
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
43@. #uring glycogen metaolism. "hos"hatase activity is regulated in (hich (ay;
!. Phos"hatase is "hos"horylated y "rotein +inase ma+ing it inactive.
$. Inhiitor51 is "hos"horylated y "rotein +inase and the "hos"horylated inhiitor inhiits "hos"hatase.
%. %yclic !4P inds to an allosteric site on the "hos"hatase. and this inhiits "hos"hatase.
#. !4P allosterically inhiits "hos"hatase.
&. The "hos"hate on the inhiitor is hydroly1ed to give a active inhiitor.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
431. 9hich of follo(ing is 0:T T/L& of histones;
!. They are small. asic "roteins
$. They are found in nucleosomes in a ratio of 1)1)1)1 ,3!),3$),8),4
%. They are only associated (ith transcri"tionally active #0!
#. They form a core of "roteins aout (hich #0! (ra"s aout 1.> times
&. They are aundant in eu+aryotic chromatin
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
433. 9hich of the follo(ing is administered after treatment (ith dihydrofolate reductase inhiitors to
"revent death due to the loss of active forms of folate;
!. allo"urinol
$. folic acid
%. methotrexate
#. thymidylate
&. leucovorin
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
438. The citric acid cycle -T%! cycle2 is regulated at (hich three ste"s;
!. %itrate synthase. aconitase. and isocitrate dehydrogenase
$. %itrate synthase. aconitase. and al"ha +etoglutarate dehydrogenase.
%. !conitase. succinate dehydrogenase. and isocitrate dehydrogenase.
#. Isocitrate dehydrogenase. al"ha +etoglutarate dehydrogenase. and citrate synthetase.
&. *umarase. succinate dehydrogenase. aconitase.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
434. Beucovorin is administered
!. To inhiit xanthine oxidase and reduce uric acid "roduction
$. To re"lace active forms of folate after treatment (ith dihydrofolate reductase inhiitors
%. To inhiit rionucleotide reductase to loc+ the gro(th of certain human "athogens
#. To loc+ #0! re"lication in cells infected (ith her"esviruses
&. To loc+ the salvage of "urine metaolites y human "arasites
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
435. The target of the antiiotics in the fluoroquinolone class is
!. ty"e II to"oisomerase
$. the re"licative helicase
%. rionucleotide reductase
#. folate synthesis
&. as"artate transcaramoylase
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
436. 9hich one of the follo(ing is a *!B'& statement aout the T%! cycle;
!. It accounts for most of the caron dioxide "roduced during the total cataolism of glucose.
$. It de"ends on a continuous su""ly of 0!#.
%. GTP is formed during one reaction of the cycle.
#. :xygen is required at the committed ste".
&. !TP inhiits the committed ste".
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
43=. $rdL is a nucleoside analog that is readily ta+en u" y human cells and incor"orated into #0!. If you
add $rdL to human cells and let them re"licate their #0! 8 times. (hat fraction of the #0! strands (ill
have the analog in them -assuming no recomination2;
!. 1 out of 3
$. 8 out of 4
%. 1 out of 4
#. = out of >
&. 1 out of >
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
43>. 9hich of the follo(ing is a *!B'& statement aout the "entose "hos"hate "ath(ay;
!. This ta+es "lace in the cytosol of most cells.
$. T(o "roducts are 0!#P, and riose "hos"hate.
%. This alternative "ath(ay generates more !TP than aeroic glycolysis.
#. The flux through this "ath(ay de"ends u"on concentrations of 0!#P.
&. This "ath(ay is im"ortant in erythrocytes.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
43A. If a acterium is gro(n for many generations in the "resence of 1550 -EheavyE nitrogen2 then shifted
to medium containing 1450. after the #0! is co"ied four times. (hat fraction of the total #0! (ill e
hyrid -,)B2 in density;
!. !ll of it
$. 1J3
%. 1J4
#. 1J>
&. 1J16
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
48@. !ctivating telomerase (ould
!. ma+e telomeres shorter
$. ma+er telomeres longer
%. ma+e cells older
#. ma+e cells younger
&. ! and # are oth correct
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
481. 9hich of the follo(ing is *!B'& aout the metaolic intermediate citrate;
!. %itrate is formed from !cetyl %o! and oxaloacetate in the mitochondrial matrix.
$. %itrate activates "yruvate +inase to increase !cetyl %o! for the T%! cycle.
%. %itrate enhances !TP inhiition of "hos"hofructo+inase51.
#. The synthesis of citrate is allosterically inhiited y !TP.
&. %itrate is "ermeale to the inner mitochondrial memrane
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
483. ,o( many P:T&0TI!B translational reading frames does a doule5stranded #0! molecule have;
!. 1
$. 8
%. 6
#. A
&. 13
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
488. ! virus (ith a single5stranded /0! genome ma+es its (ay into a human cell and is ta+en directly to
the translation machinery. ,o( many "otential reading frames does this nucleic acid have;
!. 1
$. 3
%. 8
#. 6
&. A
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
484. Bactate is the final "roduct of totally anaeroic glycolysis ecause
!. the concentration of "yruvate ecomes limiting.
$. lactate is formed y lactic acid dehydrogenase.
%. "yruvate +inase is inactive under anaeroic conditions so lactate is "roduced.
#. the ratio of 0!#,J0!# ecomes high so 0!#, is used to reduce "yruvate.
&. the reaction cataly1ed y "yruvate +inase requires oxygen.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
485. 9hich of the follo(ing mutagens is more li+ely to disru"t the function of a "rotein coding region than
it is to disru"t the function of a region encoding a structural /0!;
!. ultraviolet light
$. $romo5deoxyuracil -$rdL2
%. an al+ylating agent
#. ethidium romide
&. "hotolyase
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
486. #eamination of cytosine
!. forms uracil
$. forms thymine
%. is re"aired y "hotolyase
#. is the most common germ line mutation in humans
&. $ and # are oth correct
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
48=. 9hich of the follo(ing is a *!B'& statement aout cyclic !4P;
!. This com"ound is formed from !TP.
$. %yclic !4P is converted to 5Q5!4P y "hos"hodiesterase.
%. %yclic !4P activates "rotein +inase-s2.
#. Glucagon increases the concentration of cyclic !4P in he"atocytes.
&. Insulin increases the concentration of cyclic !4P in muscle.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
48>. 9hen a human cell is damaged y ultraviolet light. the most li+ely mechanism of re"air is
!. y "hotolyase
$. y a mechanism using an !P endonuclease
%. y ase excision re"air
#. y a mechanism using a 4ut, homolog
&. y nucleotide excision re"air
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
48A. 9hich of the follo(ing mutagens is more li+ely to disru"t the function of a "rotein coding region than
it is to disru"t the function of a region encoding a structural /0!;
!. Lltraviolet light
$. &thidium romide
%. !n al+ylating agent
#. $romo5deoxyuracil -$rdL2
&. Photolyase
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
44@. 9hich one of the follo(ing is an !%%L/!T& com"arison of the "oly"e"tide hormones glucagon and
insulin;
!. $oth increase cyclic !4P in their res"ective target tissues.
$. $oth ind to extracellular rece"tors in their res"ective target tissues.
%. &ach increases in lood in res"onse to an increase in lood glucose.
#. Insulin increases cyclic !4P in muscle and fat. glucagon only increases cyclic !4P in liver.
&. Insulin. ut not glucagon. increases cyclic !4P in fat.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
441. You could increase the stringency of a 'outhern lot "rocedure y
!. /aising the tem"erature
$. /aising the concentration of 0a%l
%. Bo(ering the concentration of formamide
#. Increasing the concentration of detergent
&. Increasing the concentration of agarose
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
443. 9hen a human cell is damaged y ultraviolet light. the most li+ely mechanism of re"air is
!. y "hotolyase
$. y a mechanism using an !P endonuclease
%. y ase excision re"air
#. y a mechanism using a 4ut' homolog
&. y nucleotide excision re"air
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
448. &ach of the follo(ing are accurate com"arisons of 0!#P, and 0!#, &?%&PT *:/
!. 4ost 0!#P, is formed in the cytosol ut most 0!#, in the mitochondrion.
$. 0!#, is a direct sustrate for oxidative "hos"horylation. ut 0!#P, is not.
%. The reduction "otentials for 0!#, is greater than that for 0!#P,.
#. 0!#P, su""lies reducing equivalents for mixed function oxidases. ut 0!#, does not.
&. 0!#P, has one more "hos"hate than 0!#.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
444. !cyclovir is a chain terminator and is useful
!. to limit the si1e of P%/ "roducts
$. against her"esvirus infections
%. for determining the sequence of a #0! molecule
#. to +ill ra"idly gro(ing tumors
&. for treating "soriasis
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
445. 9hich of the follo(ing is a *!B'& statement aout "yruvate;
!. Pyruvate can e converted to lactate in a reaction requiring 0!#,.
$. Pyruvate can e converted to glucose.
%. Pyruvate dehydrogenase (ill convert "yruvate to !cetyl5%o!.
#. Pyruvate reacts (ith oxaloacetate to yield citrate.
&. Pyruvate contains 8 caron atoms.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
446. 4utations in homologs of acterial 4ut' and 4utB in humans cause
!. ?eroderma "igmentosum
$. ,ereditary non5"oly"osis colon cancer
%. !taxia telangiectasia
#. $loomQs 'yndrome
&. *anconiQs anemia
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
44=. 9hich one of the follo(ing en1ymes is more active (hen in its de"hos"horylated state;
!. Pyruvate +inase
$. Glycogen synthase
%. Glycogen "hos"horylase
#. ! and $ correct
&. $ and % correct
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
44>. 9hich "rimers (ill am"lify the target in the sequence elo( in a P%/ ex"eriment; 5Q5G!T%%!T!5
target5!%%!T!%%
!. 5Q5G!T%%!T! and 5Q5GGT!TGGT
$. 5Q5T!TGG!T% and 5Q5!%%!T!%%
%. 5Q5G!T%%!T! and 5Q5!%%!T!%%
#. 5Q5!%%!T!%% and 5Q5GGT!TGGT
&. 5QT!TGG!T% and 5Q5GGT!TGGT
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
44A. 9hat is the function of a translocase in the inner mitochondrial memrane;
!. To shuttle reducing equivalents from 0!#, formed during aeroic glycolysis.
$. To trans"ort !TP from the matrix to the cytosol.
%. To trans"ort !#P from the matrix to the cytosol.
#. To allo( the formation of a "roton gradient.
&. To trans"ort "rotons through !TPsynthase.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
45@. If t(o homologous #0! molecules have sequences that can e re"resented as !$%#&* and acdef
"artici"ate in recomination.
!. oth "roducts (ill e !$%#&*
$. oth "roducts (ill e acdef
%. neither "roduct (ill have any mismatches. only exchanges
#. resolution in the "atch configuration (ill "roduce !$%d&*
&. resolution in the recominant configuration (ill "roduce !$cd&*
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
451. The chemiosmotic ex"lanation for oxidative "hos"horylation states that
!. !TP is synthesi1ed as "rotons are "um"ed from the mitochondrial matrix.
$. Protons are "um"ed from the inner to the outer side of the inner mitochondrial memrane during
electron trans"ort.
%. The inner mitochondrial memrane is freely "ermeale to "rotons.
#. Protons are "um"ed from the cytosolic side of the inner mitochondrial memrane into the matrix during
electron trans"ort.
&. 4ore that one of the aove is correct.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
453. 9hich of the follo(ing is 0:T true regarding mismatch re"air in acteria
!. the methylated strand is cut y 4ut,
$. the mismatch is recogni1ed y 4ut'
%. the average re"air "atch is 1@@55@@ ases
#. the role of 4utB is not currently +no(n
&. the #0! strands are only hemi5methylated for a fe( minutes after re"lication
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
458. 9hich of the follo(ing is T/L& aout cytochrome c;
!. This is the only solule "art of the electron trans"ort chain.
$. This is the only "art of the electron trans"ort chain (hich transfer single electrons.
%. This is the EterminalE "art of electron trans"ort involved in the reduction of molecular oxygen.
#. This is the only heme (hich can com"lex cyanide.
&. This is the only cytochrome (hich doesnQt have a "rotein com"onent.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
454. !ll of the follo(ing methods can e used to diagnose an infection (ith ,IM. 9hich (ill "roduce a
reliale signal the soonest after infection;
!. ! 'outhern lot
$. ! 0orthern lot
%. ! 9estern lot
#. P%/
&. ! microarray
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
455. You are "lanning an ex"ression construct to force the "roduction of your ne(. im"roved version of
human gro(th hormone -hG,2 in &. coli. 9hich of the follo(ing ste"s (ould you 0:T have to ta+e in
order to insure ex"ression of this "rotein;
!. %hoose a vector (ith an origin of re"lication that functions in acteria.
$. 4a+e sure that the s"licing signals at the orders of all introns are intact.
%. Provide a "romoter for acterial /0! "olymerase in front of the hG, gene.
#. 4a+e sure that the coding sequence of hG, is fused in frame to acterial translation initiation signals.
&. !ll of the aove are required.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
456. 9hich of the follo(ing is T/L& aout creatine +inase54$ -%754$2;
!. %754$ only originates from cardiac muscle.
$. %754$ is one of three different isoen1ymes of creatine +inase.
%. This is the only dimeric isoen1yme of creatine +inase.
#. In serum. %754$ is converted into %75$$.
&. !n increase in the concentration if %754$ in serum al(ays indicates a 4I.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
45=. BetQs say you decided to get fancy and control ex"ression of the hG, gene in this clone using the
normal control sequences of the &. coli try"to"han -Tr"2 o"eron. 9hat (ould ha""en to hG, ex"ression if
you added lots of free try"to"han to the gro(th medium of cells carrying this construct;
!. hG, ex"ression (ould go do(n.
$. hG, ex"ression (ould go u".
%. 0othing (ould ha""en unless you restricted glucose in the medium as (ell.
#. Transcri"tion of hG, m/0! (ould "roceed. ut translation (ould e loc+ed.
&. 0othing. since Tr" o"eron ex"ression is not affected y try"to"han levels.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
45>. !n aove normal level of total serum creatine +inase -T5%72 could result from any of the follo(ing
&?%&PT
!. a fall off a ladder
$. extreme exertion
%. a good nightQs slee"
#. lunt chest trauma
&. a myocardial infarction
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
45A. 9hich of the follo(ing features is shared y oth #0! synthesis and /0! synthesis;
!. The "olynucleotide "roduct stays associated (ith the tem"late strand after synthesis.
$. 'ynthesis is usually idirectional after initiation at a single site.
%. ! "rimer is required for the "olymerase to initiate synthesis.
#. $oth strands are co"ied essentially simultaneously.
&. 0ucleotides are inserted ste"(ise according to the 9atson5%ric+ "airing rules.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
46@. %754$S1 -isoform S12 is descried as an isoform of %754$. 9here does %754$S1originate;
!. It is formed from %75$
$. It is formed from %7544
%. It is native to cardiac muscle
#. It is native to s+eletal muscle
&. It originates from %754$S3. (hich is defined as the native form from muscle
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
461. 9hich of the follo(ing modifications does 0:T ta+e "lace during the "roduction of mature t/0!s;
!. /otation of a uracil ase to "roduce "seudouridine.
$. 4ethylation of a uracil ase to "roduce -rio2thymidine.
%. Poly! addition at the 8Q end.
#. !ddition of some com"licated sustituents. li+e an iso"entenyl grou" to adenosine.
&. %onversion of uridine to dihydrouridine -#,L2.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
463. /ic+ (eighs aout 84@ ls. and his daily energy requirement is 8@=@ %al. ,is nutritionist s"ecifies a
diet "er day of 8@@ g "rotein. 3@@ g carohydrate. and 8@ g fat. The theoretical (eight loss for /ic+ each
day (ould e closest to
!. 1@@ g
$. 3@@g
%. 5@ g
#. >@@ g
&. 454 g
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
468. 9e loo+ed at some electron microsco"e "ictures of riosomal /0! transcri"tion in "rogress that
loo+ed sort of li+e %hristmas trees. 9hat feature of the underlying com"lex corres"onds to the trun+ that
runs the length of the %hristmas tree;
!. The s"licing machinery.
$. The 45' r/0! "recursor.
%. The "romoter for /0! "olymerase I.
#. The riosomal "roteins (aiting to e assemled.
&. The tem"late #0! -or chromatin2.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
464. 9hich metaolic "ath(ay accounts for most oxygen consum"tion during cataolism of foods;
!. !eroic glycolysis
$. :xidative "hos"horylation
%. The citric acid cycle
#. $eta oxidation
&. *ormation of methemogloin
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
465. The '&%:0# chemical ste" in the s"licing of eu+aryotic m/0! "recursors is)
!. addition of the =5methylguanosine tri"hos"hate ca".
$. addition of the "oly! tail.
%. Doining of t(o exons (ith the release of the lariat intron.
#. attac+ of the ranch"oint ! on the u"stream exon5intron Dunction.
&. not a transesterification. unli+e the first chemical ste".
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
466. *ats inherently contain more calories "er gram than carohydrates ecause
!. they are easier to digest
$. they are more reduced
%. they are easier to cataoli1e
#. they are cataoli1ed to caron dioxide
&. they are more oxidi1ed
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
46=. Imagine that you have isolated a ne( gene that you sus"ect is involved in a human genetic disease.
L"on examining the sequence of the gene and the "rotein you "redict is encoded y it. you recogni1e
three a""arent %ys3,is3 1inc finger motifs. 9hat can you reasonaly conclude from this;
!. The "rotein is li+ely to e a transcri"tion factor.
$. There is "roaly a leucine 1i""er motif neary in the "rotein sequence.
%. The "rotein is "roaly a re"ressor of transcri"tion.
#. The "rotein is li+ely a rece"tor for a steroid hormone.
&. !ll of the aove.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
46>. 9hich residue is an aromatic amino acid;
!. Thr
$. Pro
%. 4et
#. Tyr
&. ,is
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
46A. 9hich of the follo(ing is a rio1yme;
!. /0! "olymerase II.
$. m/0!.
%. Bac re"ressor.
#. 'elf5s"licing grou" I intron.
&. t/0!.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4=@. ,igh levels of lood glucagon activate gluconeogenesis and inactivate glycolysis y
!. activating fructose 1. 6 is"hos"hatase. inactivating gluco+inase. and inducing the transcri"tion of
glucose 65"hos"hatase.
$. activating aldolase and lo(ering the concentration of fructose 3.6 is"hos"hate.
%. inactivating "yruvate +inase. lo(ering the concentration of fructose 3.6 is"hos"hate and inducing the
transcri"tion of P&P caroxy+inase.
#. activating "yruvate caroxylase. inactivating "hos"hofructo+inase 1. and inducing the transcri"tion of
P&P caroxy+inase.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4=1. 9hich amino acid is 0:T a hydro"hoic residue;
!. Ile
$. leu
%. !rg
#. Mal
&. Phe
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4=3. 9hat is the most li+ely consequence of a mutation in an intron that does not change the consensus
sequences at the donor site. the acce"tor site. or the ranch"oint;
!. Termination of transcri"tion.
$. *ormation of a ne( s"lice donor site.
%. %hange of one amino acid in the corres"onding "rotein.
#. Increased level of ex"ression of the m/0!.
&. 0o effect.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4=8. Gluconeogenesis occurs
!. only in liver mitochondria.
$. only after extensive fasting.
%. until muscle "rotein is exhausted.
#. in the liver and. to a small extent. +idney.
&. y glycolysis in reverse.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4=4. 9hich residue is "ositively charged at "hysiological ",;
!. 'er
$. %ys
%. Bys
#. !s"
&. Thr
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4=5. 9hat feature is shared y "romoters and enhancers in eu+aryotic gene ex"ression;
!. There are T!T! oxes in oth "romoters and enhancers.
$. $oth are inding sites for /0! "olymerase II.
%. It doesnQt matter (hat their orientation is relative to the gene they control.
#. Their effects are mediated y sequence5s"ecific #0!5inding "roteins.
&. They al(ays cause re"ression of transcri"tion.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4=6. Glucogenic amino acids
!. are often ro+en do(n to intermediates in the citric acid cycle
$. include all amino acids exce"t lysine and leucine.
%. are released from muscle "rotein y lo( lood insulin levels.
#. include essential and nonessential amino acids
&. all of the aove.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4==. 9hat factor is 0:T an essential ste" in general "rotein folding;
!. %is5trans "e"tide ond isomeri1ation
$. Protein disulfide exchange
%. 'equestration of hydro"hoic grou"s a(ay from solvent
#. *ormation of inter5residue hydrogen onds
&. *ormation of lysinenorleucine crosslin+s
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4=>. 9hich of the follo(ing is 0:T a characteristic of acterial helix5turn5helix "roteins that regulate gene
ex"ression;
!. The recognition helix contacts #0! ases in the maDor groove.
$. The helix5turn5helix motif is the dimeri1ation domain of the "roteins.
%. The "roteins ty"ically ind to #0! as dimers. contacting consecutive maDor grooves on one face of the
#0! du"lex.
#. $oth the "roteins and their #0! inding sites are ty"ically t(o5fold -dyad2 symmetric.
&. /ecognition involves interaction et(een amino acid side chains and s"ecific ase "airs.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4=A. ! deficiency in glucose 65"hos"hatase
!. is the only cause of ty"e I glycogen storage disease -Mon Gier+eQs disease2.
$. causes severe fasting hy"oglycemia.
%. loc+s only gluconeogenesis.
#. results in decreased lactate "roduction.
&. all of the aove.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4>@. 9hat is im"ortant in the activation of 1ymogens;
!. Proteolysis of a "e"tide ond
$. !#P5riosylation
%. Glycoli"id addition
#. *ormation of salt ridges
&. !ctivity of cis5trans "roline isomerase
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4>1. 9hy does a he"atitis virus have a inding site for a liver5s"ecific transcri"tion factor;
!. !ll human diseases arise in the liver.
$. Transcri"tion occurs only in the liver.
%. The virus targets liver cells. and it needs to ex"ress its genes there.
#. Biver5s"ecific transcri"tion factors are found in all cells.
&. The virus is really an alumin gene gone ad.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4>3. 9hy does the "roduction of glucose require an energy in"ut higher than that released during
glycolysis;
!. $ecause gluconeogenesis occurs oth in the mitochondria and cytosol. and the shuttling of
intermediates requires energy.
$. This occurs so that the free energy change of the overall "rocess remains negative.
%. $ecause glycolysis has three com"letely irreversile ste"s.
#. $ecause of the connection et(een gluconeogenesis and the citric acid cycle.
&.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4>8. 9hat modification fails to occur in individuals afflicted (ith scurvy;
!. Gamma5 caroxylation of glutamates
$. !#P5riosylation
%. ,ydroxylation of Pro
#. 05terminal myristylation
&. %leavage of signal sequence
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4>4. You are designing a ne( vector that is designed to allo( regulated ex"ression of genes in
mammalian cells. 9hich of the follo(ing a""roaches has essentially 0: ho"e of (or+ing;
!. Put a acterial terminator sequence in the middle of the gene. and control ex"ression y modulating
Bac re"ressor levels (ith IPTG.
$. Put an iron res"onse element from the transferrin rece"tor gene into the 8Q5LT/ of the ex"ressed
m/0!. and control m/0! staility (ith iron levels in the gro(th medium.
%. Put a inding site for the glucocorticoid rece"tor in the "romoter of the gene. and control transcri"tion
y a""lying or (ithholding glucocorticoid hormones.
#. Put a inding site for the heat shoc+ transcri"tion factor in the "romoter of the gene. and control
transcri"tion (ith tem"erature.
&. !ll of the aove (ill (or+.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4>5. ,igh levels of ethanol ingestion inhiit glucose iosynthesis y
!. "reventing the utili1ation of "yruvate. glycerol and intermediates of the citric acid cycle from eing
utili1ed as "recursors
$. inhiiting the induction of P&P caroxy+inase.
%. increasing the 0!#<J0!#, ratio.
#. "roducing acetate. from oxidation of ethanol in the liver. (hich inhiits "yruvate caroxylase.
&. all of the aove.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4>6. 9hich is 0:T true of "rotein secondary structures;
!. ,ydrogen onding in an al"ha helix occurs et(een residues (ithin the helix
$. ,ydrogen onding in eta sheets occurs "rimarily et(een side chains of alternating residues
%. !m"hi"athic helices have se"arate hydro"hoic and hydro"hilic surfaces
#. Parallel eta sheets tend to have oth surfaces hydro"hoic
&. !nti"arallel eta sheets are often connected y short reverse turns
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4>=. 9hat cellular com"onent-s2 is-are2 res"onsile for recogni1ing s"lice sites in m/0! "recursors;
!. t/0!s.
$. sn/0Ps.
%. /0! "olymerase II.
#. Poly! "olymerase.
&. 'teroid rece"tor "roteins.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4>>. #erivatives of vitamin $6 -"yridoxine2 are essential for)
!. the "yruvate caroxylase reaction.
$. transaminase and decaroxylation reactions of amino acids.
%. the hydroxylation of "henylalanine. tyrosine and try"to"han.
#. all of the aove.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4>A. In (hat (ay are amino acid side chains oriented in an al"ha helix;
!. 'ide chains "roDect to(ard the interior of al"ha helices
$. 'ide chains "roDect out(ard from the helical axis
%. 'ide chains alternate "roDecting in(ard and out(ard
#. 'ide chains sho( no "reference in their orientation
&. 'ide chains "roDect to(ard only one face of the helix. the side facing the solvent
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4A@. 9hich of the follo(ing is T/L&;
!. m/0! is read 8Q to 5Q. and "rotein is synthesi1ed %5terminus to 05terminus.
$. m/0! is read 5Q to 8Q. and "rotein is synthesi1ed %5terminus to 05terminus.
%. m/0! is read 8Q to 5Q. and "rotein is synthesi1ed 05terminus to %5terminus .
#. m/0! is read 5Q to 8Q. and "rotein is synthesi1ed 05terminus to %5terminus.
&. m/0! can e read either 8Q to 5Q or 5Qto 8Q.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4A1. The "ur"ose of the urea cycle is to convert ammonium into a solule. non5toxic form.
!. True
$. *alse
%.
#.
&.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4A3. 9hat is T/L& aout chain turns -reverse turns2 in "oly"e"tides;
!. %hain turns ty"ically occur in the interior of "roteins
$. %hain turns tend to have a"olar residues
%. %hain turns are usually helical
#. %hain turns occur on the surface of "roteins
&. %hain turns tend to have the im"ortant catalytic residues
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4A8. 9hich of the follo(ing is T/L& for oth "ro+aryotes and eu+aryotes;
!. m/0! is modified y a 5Q methylguanylate ca".
$. m/0! is modified y addition of a "oly! tail.
%. The small riosomal suunit inds to the 'hine5#algarno sequence.
#. The first codon is al(ays !LG -i.e. codes for 4et2.
&. /iosomes are made of "rotein and #0!.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4A4. Genetic defects in the urea cycle cause disease "rimarily ecause they result in liver damage.
!. True
$. *alse
%.
#.
&.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4A5. 9hat is 0:T true aout the tertiary structure of "roteins;
!. 'ome "roteins are "redominantly al"ha helical
$. 'ome "roteins are formed "rimarily y anti"arallel eta strands
%. 'ome "roteins are a mixture of al"ha helical and eta structures
#. Gloular "roteins tend to have hydro"hoic interiors
&. Proteins interiors usually have a numer of cavities for inding of glucose
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4A6. 9hich of the follo(ing is T/L&;
!. Production a charged t/0!s requires hydrolysis of GTP y amino t/0! synthetases.
$. The fidelity of some amino t/0! synthetases is enhanced y editing.
%. %harged t/0! molecules are ound y &*5Tu. (hen &*5Tu is also ound to G#P.
#. Inhiitors of acterial riosomes are never used as antiiotics ecause they also inhiit human
riosomes.
&. t/0! molecules ind their activated amino acid residues through their anticodon loo"s.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4A=. 0eonatal Daundice can e dangerous ecause
!. heme cannot e "ro"erly synthesi1ed in these infants.
$. iliruin diglucuronide cannot e excreted.
%. unconDugated iliruin can enter the rain.
#. these infants cannot "roduce enough vitamin # (ithout "hotothera"y.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4A>. The inding of $PG to hemogloin occurs "rimarily y (hich of the follo(ing;
!. ,eme iron
$. Gamma chain
%. !l"ha chain
#. $eta chain
&. !l"ha amino ends of each chain
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
4AA. 9hich of the follo(ing is T/L&;
!. The genetic code of mammals if different from that of &. coli.
$. &xons are segments of genes that are 0:T ex"ressed in the resultant "rotein molecule.
%. Introns and &xons are common in acteria.
#. /iosomal frameshifting allo(s one segment of the ,IM genome to code for more than one "rotein
molecule.
&. ,ydrolysis of GTP is required for the initiation and termination ste"s of "rotein translation. ut not for
elongation.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
5@@. Phenyl+etonuria results in the "roduction of toxic "henylalanine metaolites that are not normally
found in the ody.
!. True
$. *alse
%.
#.
&.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
5@1. 9hat most accurately descries the function of the "roximal ,is in hemogloin;
!. Proximal ,is is one of the im"ortant residue in hydrogen onding to $PG
$. Proximal ,is is derivati1ed (ith caron dioxide
%. Proximal ,is is the residue that confers the maDor $ohr effect
#. Proximal ,is hydrogen onds the incoming dioxygen molecule
&. Proximal ,is coordinates the heme iron ion
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
5@3. 9hich of the follo(ing is the T/L& cause of I5cell disease;
!. *ailure of "roton "um"s to acidify lysosomes.
$. *ailure of clathrin to form trans"ort vesicles.
%. &ating too much cheese.
#. !sence of a 7#&B sequence on an &/ "rotein
&. *ailure to "hos"horylate a mannose grou"s in the cis Golgi.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
5@8. 9hich of the follo(ing is 0:T a neurotransmitter "roduced y amino acid decaroxylation)
!. nore"ine"hrine.
$. g5aminoutyrate.
%. e"ine"hrine
#. acetylcholine
&. serotonin.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
5@4. 9hat is 0:T im"ortant in the coo"erative inding of dioxygen to hemogloin;
!. %oncentration of methemogloin reductase
$. %oncentration of $PG
%. %oncentration of hydrogen ions
#. %oncentration of caron dioxide
&. %oncentration of chloride ions
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
5@5. 9hich of the follo(ing is T/L&;
!. Iron5loaded transferrin is internali1ed y rece"tor5mediated endocytosis and targeted to the nucleus.
$. Transferin and its rece"tor dissociate at the lo( ", of endosomes.
%. &ndocytosed "roteins and rece"tors are sorted in mitochondria.
#. B#B rece"tors are usually degraded follo(ing their endocytosis.
&. Transferin rece"tors are usually returned to the cell surface follo(ing their endocytosis
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
5@6. !rgininosuccinate lyase deficient "atients excrete argininosuccinate into the urine. 9hy are arginine
su""lements an effective "art of their treatment;
!. The arginine can e hydroly1ed y arginase to re"lace de"leted ornithine.
$. !rginine can serve as a Esin+E for free ammonium.
%. $ecause hydrolysis of arginine "roduces urea.
#. all of the aove.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
5@=. 9hat descries the sliding contacts in the hemogloin tetramer;
!. Interaction of al"ha chains
$. Interaction of eta chains
%. 4ovement of "roximal ,is along axis of * helix
#. Interaction of al"ha1.eta1 chains
&. Interaction of al"ha1.eta3 chains
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
5@>. 9hich of the follo(ing is T/L&;
!. The cytosolic ,s"=@ cha"erone does not function in the im"ort of "roteins into mitochondria.
$. 05terminal signal sequences are cleaved from large "roteins follo(ing their im"ort into the nucleus.
%. The nuclear and &/ memranes are contiguous (ith each other.
#. Barge "roteins can diffuse freely et(een the nucleus and cytosol.
&. !ll of the aove are true.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
5@A. *rogs egin life as tad"oles in an aqueous environment. !s they mature. they convert from eing
largely ammonotelic to eing ureotelic. 9hich of the follo(ing en1yme activities (ould you ex"ect to
increase dramatically as frogs mature;
!. Glutaminase
$. !lanine aminotransferase
%. Glutamine synthase
#. &ntero"e"tidase
&. %aramoyl "hos"hate synthetase I
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
51@. 9hich is 0:T true aout mutant hemogloin molecules in sic+le cell anemia;
!. Preci"itation of deoxyhemogloin
$. Glu to Mal sustitution on the surface of eta chains
%. %an e com"ensated y increase ex"ression of fetal gamma chains
#. *ier formation of oxyhemogloin
&. Tendency to "reci"itate can e reversed y modification of al"ha amino grou"s
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
511. 9hich if the follo(ing is T/L&;
!. $inding of signal recognition "article to a signal sequence results in arrest of translation.
$. %ore oligosaccharide is added to "roteins in the cytosol.
%. %alnexin is a mitochondrial cha"erone.
#. Mesicles destined for the cell surface are usually traffic+ed through lysosomes efore going to the
"lasma memrane.
&. &xtracellular "roteins are synthesi1ed y riosomes that are attached to the "lasma memrane.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
513. 9hat is 0:T an im"ortant feature in the structure of tro"ocollagen;
!. ,ydroxylation of "roline
$. Gly residue every third residue
%. #isulfides lin+s et(een chains
#. Bysinenorleucine crosslin+s
&. ,ydroxylation of lysine
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
518. 9hich of the follo(ing is T/L&;
!. The ' "hase of the cell cycle is immediately follo(ed y G1.
$. #0! re"lication occurs during mitosis.
%. The G1 and G3 chec+"oints monitor external environments -e.g. gro(th factor signals2 and internal
signals such as cell si1e and integrity of the #0!.
#. G@ is an accelerated form of the G1 "hase that allo(s for accelerated "rogression through the cell
cycle.
&. %hromosomes are condensed throughout inter"hase. ut ecome decondensed in order to "ass the
meta"hase5ana"hase chec+"oint.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
514. 9hat is 0:T an im"ortant feature of en1yme catalysts;
!. &n1ymes lo(er the activation energy arrier
$. &n1ymes shift the equilirium of a reaction to "roduct formation
%. &n1ymes are com"lementary to sustrate transition states
#. &n1ymes ind sustrates y (ea+ noncovalent interactions
&. &n1ymes are active (ithin a narro( ", range
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
515. 9hich of the follo(ing is T/L&;
!. %d+ en1ymes are activated y cyclins.
$. The activity of %#7 en1ymes is regulated y "hos"horylation.
%. %yclins are degraded y the uiquitin5"roteosome "ath(ay.
#. %d+s "hos"horylate. and therey activate. some "roteins that function to further stimulate %d+ activity.
&. !ll of the aove are true.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
516. 9hat is T/L& of the function of the catalytic triad in chymotry"sin;
!. !s"1@3 and ,is5= activate 'er1A5
$. !s"1@3. ,is5= and 'er1A5 form the sustrate inding site
%. ,is5= and 'er1A5 activate !s"1@3 for nucleo"hilic attac+
#. !s"1@3. ,is5= and 'er1A5 activate a (ater molecule for hydrolysis of the "e"tide ond
&. !s"1@3. ,is5= and 'er1A5 staili1e the structure of the chymotry"sinogen 1ymogen enaling 1ymogen
activation
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
51=. 9hich of the follo(ing is T/L&;
!. !ctin often functions to sha"e the cell surface.
$. 7inesin and #yneins are motor "roteins that move along actin filaments.
%. !ctin filaments radiate out from the centrosome.
#. Polymeri1ation and de"olymeri1ation of actin involves a cycle of GTP inding and hydrolysis.
&. Polymeri1ation of actin requires ra"id synthesis of ne( actin molecules.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
51>. The inhiitory effects of a noncom"etitive inhiitor on an en1yme are overcome y (hich of the
follo(ing treatments;
!. Increasing the sustrate concentration
$. Increasing the tem"erature of the reaction
%. %ross5lin+ing the en1yme side chains
#. !ll of the aove
&. 0one of the aove
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
51A. 9hich of the follo(ing is T/L&;
!. :nce formed. microtuules are generally stale for the lifetime of the cell.
$. %entrosomes re"licate and divide to form the "oles of the s"indle ody.
%. The nuclear memrane remains intact throughout the mammalian cell cycle.
#. %yto+inesis only starts after telo"hase is finished.
&. In mitosis. one cell divides to create t(o gametes.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
53@. The citric acid cycle -T%! cycle2 is initiated y the condensation of t(o molecules (hich are
!. 0!# and oxaloacetate.
$. "yruvate and caron dioxide.
%. acetyl %o! and caron dioxide.
#. acetyl %o! and oxaloacetate.
&. "yruvate and !TP.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
531. This is the organ or tissue (hich only uses glucose in the fed state or during starvation.
!. adi"ose tissue
$. rain
%. s+eletal muscle
#. liver
&. erythrocytes
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
533. This is the main site of synthesis for +etone odies during starvation.
!. adi"ose tissue
$. rain
%. s+eletal muscle
#. liver
&. erythrocytes
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
538. These tissues require insulin to facilitate glucose trans"ort into cells. !. adi"ose tissue $. rain %.
s+eletal muscle #. liver &. erythrocytes
!. ! Y $
$. $ Y %
%. % Y #
#. # Y &
&. ! Y %
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
534. In these tissues. adenylate cycle (ill e stimulated y oth glucagon and e"ine"hrine. !. adi"ose
tissue $. rain %. s+eletal muscle #. liver &. erythrocytes
!. ! Y $
$. $ Y %
%. ! Y #
#. # Y &
&. $ Y #
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
535. The glucocorticoids
!. stimulate adenylate cyclase in liver.
$. alter rates of "rotein synthesis.
%. inhiit gluconeogenesis.
#. stimulate glycolysis.
&. inhiit oxidative "hos"horylation.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
536. 9hich one of the follo(ing is 0:T a characteristic of the hexose mono"hos"hate "ath(ay;
!. %aron dioxide is "roduced.
$. It forms 3 !TP "er glucose oxidi1ed.
%. It "roduces riose555"hos"hate.
#. It "roduces 0!#P,.
&. The first reaction is controlled y the concentration of 0!#P,.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
53=. 9hich one of the follo(ing conditions in the matrix of a mitochondrion (ould decrease the oxidation
of !cetyl %o! in the T%! cycle;
!. ! lo( ratio of !TPJ!#P.
$. ! high concentration of !4P.
%. ! high ratio of 0!#,J0!#.
#. ! lo( ratio of GTPJG#P.
&. ! high concentration of oxaloacetate.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
53>. In human liver. fructose is "hos"horylated to give fructose515"hos"hate. This is follo(ed y
!. "hos"horylation to give fructose51.65is"hos"hate.
$. conversion to fructose565"hos"hate.
%. cleavage to form glyceraldehyde and dihydroxyacetone "hos"hate.
#. isomeri1ation to glucose515"hos"hate.
&. hydrolysis to give fructose.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
53A. The en1yme cataly1ing the rate limiting reaction of glycolysis
!. is activated y higher !TP.
$. cataly1es a reaction (hich is reversile.
%. is inhiited y fructose53.65is"hos"hate.
#. is activated y higher citrate.
&. uses fructose565"hos"hate as a sustrate.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
58@. The surest treatment for a "atient (ho accidentally ingested antifree1e (ould e to
!. infuse sodium nitrite and then use amyl nitrate inhalation.
$. give a fructose rich drin+ li+e Lltra *uel.
%. give a cou"le shots of scotch (his+y.
#. give t(o cu"s of strong coffee.
&. give a drin+ (hich is enriched in citrate.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
581. &ach of the follo(ing is ca"ale of increasing the activity of muscle glycogen "hos"horylase &?%&PT
*:/
!. e"ine"hrine.
$. calcium ions.
%. active "hos"horylase +inase.
#. glucagon.
&. cyclic !4P.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
583. &ach of the follo(ing is generally true aout 0I##4 &?%&PT that
!. it is accom"anied y "olydi"sia and "olyuria.
$. it is associated (ith oesity.
%. no insulin is detected in serum.
#. there is moderate to high glucose in serum.
&. there is a strong genetic com"onent.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
588. E:xidative stressE refers to
!. the fact that oxidative "hos"horylation requires !#P.
$. the fact that oxidative "hos"horylation requires molecular oxygen.
%. the failure of aeroic glycolysis to meet the energy demands of muscle.
#. the uncou"ling of oxidative "hos"horylation.
&. the formation of free radicals ecause of the im"erfect reduction of oxygen to give (ater.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
584. Miagra o(es its efficacy to the fact that it
!. activate adenylate cyclase in smooth muscle.
$. stimulates glycolysis.
%. stimulates guanylate cyclase.
#. inhiits cyclic G4P "hos"hodiesterase.
&. stimulates oxidative "hos"horylation.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
585. The inding of insulin to rece"tors on he"atocyte causes each of the follo(ing &?%&PT
!. increased activity of tyrosine +inase.
$. increased activity of glycogen "hos"horylase.
%. increased synthesis of glycogen.
#. increased synthesis of fatty acids.
&. increased glycolysis.
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
586. &ach of the follo(ing statements aout the "rotein com"lex that carries out the synthesis of !TP
during oxidative "hos"horylation is correct &?%&PT
!. it contains a "roton channel.
$. it is inhiited y oligomycin.
%. it inds molecular oxygen.
#. it is emedded in the inner mitochondrial memrane.
&. !TP synthesi1ed y this com"lex is released to the matrix.
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
58=. !fter 5 days of starvation all of the follo(ing (ould e true &?%&PT
!. the rain -nervous system2 (ould only use +etone odies for energy.
$. glycogen in liver and muscle (ould e totally de"leted.
%. most circulating glucose (ould come from he"atic gluconeogenesis.
#. the ratio of insulinJglucagon (ould e much lo(er than efore the fast.
&. glucagon (ould increase the release of fatty acids from adi"ocytes.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
58>. !cetyl %o! is descried y all of the follo(ing &?%&PT
!. itQs formed y the "yruvate dehydrogenase com"lex.
$. it condenses (ith oxaloacetate to give citrate.
%. the acetate carons of acetyl %o! are incor"orated into fatty acids.
#. it enhances the "hos"horylation of "yruvate dehydrogenase.
&. it is the end "roduct of glycolysis.
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
58A. The drug !ntause -disulfiram2
!. inhiits the com"lete oxidation of ethyl alcohol.
$. inhiit isocitrate dehydrogenase.
%. uncou"les oxidative "hos"horylation.
#. inhiits electron trans"ort.
&. inhiits "yruvate dehydrogenase.
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
54@. 9hat is 0:T true aout the staility of a gloular "rotein;
!. ,ydro"hoic grou" are shielded a(ay from solvent
$. ,ydrogen onding et(een residues s"atially se"arated in sequence
%. Boo" structure connecting secondary structural elements are on the surface and hydrogen onded to
(ater
#. !ll "e"tide ond caronyl oxygens and amides are hydrogen onded to solvent or to other "oly"e"tide
donorsJacce"tors
&. !ll aromatic rings are stac+ed giving "i electron resonance
'ho( ans(er
%orrect !ns(er) &
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
541. 9hat is 0:T true aout the aility of hemogloin to ind oxygen;
!. &ach suunit inds one heme grou"
$. Proximal methionine inds heme ferrous ion activating it for oxygen inding.
%. *errous iron in heme grou" inds to oxygen
#. ,eme iron is shielded from solvent +ee"ing iron as ferrous
&. ,emogloin is "resent in erythrocytes (hich "ass through lung for oxygenation
'ho( ans(er
%orrect !ns(er) $
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
543. 9hat is 0:T im"ortant for the deoxygenation of hemogloin;
!. $inding of four is"hos"hoglycerates "er hemogloin tetramer
$. Protonation induced salt ridge formation et(een suunits
%. $inding of caron dioxide and induced formation of salt ridge et(een suunits
#. Increase in the numer of suunit contacts et(een a31 a13 suunits
&. %oo"erativity et(een hemogloin suunits
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
548. 9hat is 0:T true of an en1ymeQs aility to e a catalyst;
!. &n1ymes can s"ecifically ind sustrate molecules.
$. $inding of sustrate induces a strain in the sustrate molecule.
%. &n1ymes lo(er the energy arrier in the conversion of sustrates to a transition state
#. &n1ymes shift the equilirium et(een sustrates and "roducts
&. &n1ymes have s"ecific residues in the active site ca"ale of carrying out acidJase chemistry or
covalent catalysis.
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
544. 9hat is 0:T a (ay "roteins are modified "ost5translationally;
!. %leavage of a "oly"e"tide ond
$. 4odification of the 05terminal residue
%. !cetylation of "e"tide ond caronyl oxygens
#. !ddition of com"onents to the %5terminus
&. %rosslin+ing of certain residues
'ho( ans(er
%orrect !ns(er) %
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
545. 9hat is 0:T a common (ay an en1yme can e inhiited;
!. y com"ounds that increase the Mmax of the en1yme
$. y com"ounds that increase the 7m of the en1yme for a sustrate
%. y com"ounds that destaili1e the en1yme
#. y com"ounds that "ertur oth the Mmax and 7m "arameters of an en1yme
&. y other en1ymes that covalently modify the "articular en1yme
'ho( ans(er
%orrect !ns(er) !
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)
546. 9hich of the follo( does 0:T descrie ho( mutations often attenuate the function of "roteins;
!. mislocali1ation of "rotein
$. destaili1ation of "rotein
%. misfolding of the "rotein
#. increasing the numer of disulfide lin+ages
&. removal of nucleo"hilic residues in en1ymes
'ho( ans(er
%orrect !ns(er) #
*eedac+ !)
*eedac+ $)
*eedac+ %)
*eedac+ #)
*eedac+ &)

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BIOCHEMISTRY TEST

You have 546 questions in this exam.

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