RafflesJuniorCollege CoreSyllabus- BioMolecules JC22008

EXAMPLES ofCARBOHYDRATES
1. GLUCOSE 2. GALACTOSE 3. FRUCTOSE
a-glucose i3-glucose
s:
'CH,OH
o
:::J
o
(f)
HOH2Q1C 0 .....
8
'"
2 5 :::r

Ci
3 4 6CHPH CD
(f)
H OH H OH H OH
Fructose=C2 contains
Glucose & Galactose=C1 contains aldogp(makingthem aldehydes)
keto gp(making it aketone)
1. MALTOSE(0-1,4 glycosidicbond)
a-glucose + a-glucose
'CH,OH 'CH,OH
o
(ii'
()
()
'"
:::r

Ci
CD
(f)
'I 'I
H OH H OH
maltose

+
2. LACTOSE(13-1,4 glycosidicbond) f3-galactose +a-glucose
3. SUCROSE(0-1,2 glycosidicbond) a-glucose+f3-fructose
1. STARCH (plant) - a-glucosemonomers
Amylose Amylopectiin
> 9 '

branches ofhelices
. til
cfJ
linkedby0-1,6 glycosidic
!..
",
d4
..

all monomerswithin helix V't'
all monomerswithin helix
linked by 0-1,4glycosidicbonds linkedby 0-1,4 glycosidicbonds
e,:X)
,.

.
2. CELLULOSE(plant) - f3-glucose monomers
"'0
o
"""all monomerswithin chain linked by 13-1,4 glycosidicbonds,
-<
(f)
making everyaltematemonomer/residue
()
'"
()
inverted in orientation
:::r

Ci
CD .straightchains cross-linked by Hbonds (interchain)
(f)
3. GLYCOGEN (animal)- a-glucosemonomers fI'!", ... '"ZL
branches ofhelices ....
linked by 0-1,6glycosidicbonds ......".. .. "".....
IltJ.. all monomerswithin helix
'\J linked by 0-1,4glycosidicbonds
Lastuodatedby: Mrs Maodatene Tan &Mrs Jeanne Wan
COMMON FEATURES
1.All are hexoses(6C) .
2.Allcarryonecarbonylgp
(eitheraldo- orketo- gp)
3.Can existas 6or5-
membered ring
4.Ring structuresexhibit
a- and13- isomerism
(OH grpatC1: a- below,
j3 - above)
5. Soluble, sweet,
6. All are reducingsugars
7.Basicunitofcarbohydrates
1. Made up of2monomers
2.Monomers linktoeach other
via condensationreaction
to produce adisaccharide
and aH20 molecule
via varioustypes of
glycosidicbonds
3.Splitting ofadisaccharide
into its componentmono-
saccharidesvia hydrolysis
and uses 1Hp
4. All are reducingsugars
exceptsucrose
1. Madeup of1OOs - 1000s
monomers
2.Monomers linkto each other
via condensationreaction
to produce apolysaccharide
and H20s
via varioustypes of
glycosidicbonds
3.Splitting ofapolysaccharide
into itscomponentmono-
saccharidesvia hydrolysis
and uses H20s
4.Generallycategorised based
on function into
(i) STORAGE
Polysaccharide
(starch: amylose &
amylopectin; glycogen) &
(ii) STRUCTURAL
polysaccharides(cellulose)
STRUCTURE FUNCTION
1. SmallMr/Smallin size+manyOH groupsextending out
ofthering
readilysolublein water+easilytransported in animal and
planttransportsystems
2.Carbonyl group
possessareducingproperty
3. Exhibitsisomerism
contributesto diversityofmonomers diversityof
polymers
1. SmallMr/Smallin size +manyOH groupsextending out
oftherings
readilysolublein water+easilytransported in transport
systems(esp. in plants: sucrose)
2.Some possessa free carbonyl group
possessareducingproperty(exceptsucrose)
STARCH (amylose) - Storage
1.Made up ofmanya-glucose residues
large energystore
insoluble/slightlysoluble in water, 4Jw ofcells unaffected
2.Linearchains coiled intohelices
possiblymorecompact:more moleculesperfixed voL
3. 0(1 glycosidiclinkagesbetween residues
hydrolysisviaspecificenzymeswhen needed
CELLULOSE- Structural
1.Made up ofmanyf3-glucose residues
large, insolubleandwill notaffect4Jwofcells
2. glycosidiclinkages
hydrolyticenzymeslimited to certain organisms, so not
commonlyhydrolysed source ofourdietaryfibre?)
3.Each residue is rotated 180,makingevery altemate
residue inverted in orientation
OH groupsproject outwards in all directions
H-bondswith adjacentparallelmolecules
H-bondcross-linkingbetween cellulose molecules
rigid structurewith high stability
4. Astructural hierarchypresent
(molecules microfibrils macrofibrils)
reinforces structureto givehightensilestrength
fullypermeablemeshofseveral layers
free movementofwaterand solutes
GLYCOGEN- similarto amvlose, butmore highlybranched
AMINOACIDS AMINOACIDS(MONOMERS) -7 POlYPEPTIDES (POLYMERS) -7 PROTEINS EXAMPLESOF PROTEINS/STRUCT -7 FN
Properties ofaminoacids -0 1.Uniquesequenceand numberofamino acids Hierarchyofprotein structure 1. Form long chains
1. Basicunitofproteins . in apolypeptide 2. Stable,regularstructure
'<Q. ,PG' . '. < Primarystructure
2. 20 differenta.a. in cells III 2. Linked by covalentpeptidebonds 3. Insolublein water
3. All possess 1acarbon atom, bonded to: -< 3. E.g. ofaportion ofaprimarystructure:
0,,!,. .r........:.."l... .. .. .r: .....
4. Secondary structure important
. .@M)
Pd, ,, ,,y ." ;' H H
- 1carboxyl group, ., .- gly- ser- his- val- gly- ala - ... """,,'.
1
1 i V S. Usuallyplaystructural role
- 1aminogroup, 1'i 4. The secondary, tertiaryand quaternary
I)L.... I ! r ......i. .
- 1Hatom structuresare hencedirectconsequences of
COLLAGEN
- 1Rgroup: varies with differenta.a. and (I) the primarystructure
t V ..,
can be ahydrophobic, hydrophilic,
.."
0
5'
acidic alkaline side group) 1. Intramolecularhydrogenbondsformed at secondary structuret._
..,
1. Each polypeptide chain is ahelixwith -1000
o
, H regularintervalsalong polypeptidebackbone I: residues-7 triplehelixstructure
.
VI
' I 0
'0
(calledtropocollagen)-7 large
. / N f - C,
2.
backbone(CO-NH)
Bondsonly involve atoms
Le. atomsofRgroups
ofpolypeptide HO
Hence function: insolublein water
amino H R OH carboxyl W notinvolved
2. Hbondsbetween the 3polypeptides -7
group group 8 4. 2types: ALPHAHELIX
(fj
::l
tropocollagen-7 covalentbondsbetween
R-group a. -7H bonds form betweenHand0
staggeredtropocollagen molecules -7
l
4. Soluble &exists aszwitterions(have atoms4a.a. apart(i.e. Hbelongsto collagen fibril -7 collagen fibre

f3 pleated sheet
both basicand acidicproperties) NH ofa.a.1, 0 belongsto C=O ofa.a.S) Hence function : noweak spot running through
in solution 2 -7 H-bonds11 to longitudinalaxis fibril + large bundle produce arope-like
!l. ofhelix
structure ofgreattensilestrength
-73D helical structure
S. Hence, actas buffers
-7Structure supportsits STRUCTURALfunction
BETAPLEATED SHEET
(resistssmall changes in
to givefirmness and to skin
H I
-7 Hbondsform between segments of
tertiary ?
the polypeptidewhich are parallelto
structure H R
1. Form spherical, compact shapes each other -7 3D accordion-likesheet
(Note: secondary
2. lessstable, less regularstructure H
structures

1. 4key intramolecularbondsformed along
can be found 3. Soluble in water
*
@
.wl
H
(.OH
----J......
polypeptide(i.e.bondsformed within the within) 4. Tertiary structure important
09
J
,o- same polypeptide) -7 hydrophobicinteraction S. Common e.g.enzymes, blood proteins

<H bonds<ionicbonds<disulphidebridges
6. Each a.a. will have itsown isoelectric iij'
2. Formed at irregularintervals HIVProtease
point(pH atwhich each a.a.is electrically -<
3. Bondsinvolve atoms ofRgroupsonly(Le. the
quaternary
neutral) dueto uniqueRgroups
hydrophobicRgroup of(e.g.)a.a.1 will interact structure
7. Amino acids undergo condensation 1'i
withthe hydrophobicRgroup ofe.g. a.a. 78 and (Note: the
reactionto form polypeptides. The
hence pullthe 2a.a. closetogether)
polypeptideis
G> reverse occursvia hydrolysis. (I)
justone ofthe subunits)
-7 3D irregularcontortionsofthe polypeptide 0'
c-
AmlnoAcld N'nlnoAdd
l: 1. Consist oftwoidentical polypeptides(99aa)
Bondsmaking up thetertiarv structure:
H 0 H 0
-7 homodimer
I II I 11 o
Two Arn IhQ
H-N-Q--C--QH I:
1. Intermolecularbondsformed between 2or
H--N--C-C--OH '0
.., 2. Terminal domain imptfor stabilising active
AddS
I I
III
o I I more polypeptides(i.e between subunits)
HIVenzyme
H ", H R2 @" CD
::l
2.Maintained by4key bonds: Hbonds,
5' 3. At interface of2domains is the active site with
III
Condensation
ionicbonds,disulphidebonds,hydrophobic
VI
specific3D conformation- compriSing of2 >OH
-<
"",-er
reverse:hydrolysis) VI
interactions,others (notin yoursyllabus)
l'Iydws,vn
groups ofthree amino acids (asp-thr-gly)
.... \"md
. . ...;).;........::....., ..,
-7 involvein catalysis Peptide bond H ; 0 i HO'
I:
o
.. I1I1 ..1Ill:'; -7 allowsentry ofwaterand viral polyprotein

e-
H:-- H--C-+-C-- H-i-C-o::--:.OH
for hydrolysisofpeptide bond
.I Ii Ii I
H RI: H; R2 -7 enzyme specificity
t ,................
3D shape ofaprotein may be changed by:
4. 2flexibleflapsguard active sites -7 exclude i
a
1.Heat
HtermIOlS
moreincoming water molecules -7 this allows
3. Inorganicchemicalse.g. heavymetals
2.Acids/Alkalis (pH)
catalyticreaction to occur
/
/
S. ENZYMATICfunction:to cleave polyproteins .. 4. Organicchemicalse,g. ether, alcohol
intofunctional viral proteins S.Mechanicalforces
2
EXAMPLESOFLlPIDS
1.Each is made up ofglyceroland fatty acids
1glycerol + 3fattyacids 1triglyceride (via condensation ofcomponents)
H
HtOH
I
Il - C- Oll
I
HMCOIl
I
-l
.., H
to'
-<
n
<tl
..,
1glycerol +

H.. C.. OH
i
::r Ile" OH
"tl
o !
I/l If ' C.. OH
"C
I
::r
H
g,
"C
a:
... "".. """"", esterlinkages

n
., . An or,:'j trig!yccrkle .
o o ,
Ii/,i ' / ' . /'/" A .,
..:-::S:')'/ \, v ', V \/'\.
1I
o
;"" " \
HO,wO-l' lI i<-
6,... .... . ...
hydrocarbon tail
a: 2. Hence, atriglyceridemolecule has ahydrophi lic'head'and a hydrophobic'tail'
<tl
I/l 3. Insolubleinwater(exists asmicelles); soluble in organicsolvent
4. 2types:Saturated Fat Unsaturatedfat
1. lacksC=Cin hydrophobictails 1. possess 1or>1 C=C kinks in tails
2. quiteclosely packed solid at room temp 2. kinks preventclose packing liquid at room temp
3. usuallyfound in animals 3.usuallyfound in plants and fish
4. e.g.bacon grease, lard, butter 4. e.g. vegetable oil, cod liveroil
O'C

1.Each is made up ofglycerol, fatty acids and phosphategroups
2fattyacids + 1phosphate grp
1l0-'OM' 1I OH
tI I
0 OH- P-OH
1I
0
cl
I
phosphoesterlink........::1-'...!!
. bH
1phospholipid + 3H20

1

lH.COO
OH
I

I/l 2. Hence, it has ahydrophilicphosphate 'head' (also cos of-vecharge) and ahydrophobic hydrocarbon'tail
3. Such aproperty makesit an amphipathicmolecule
4.Insolubleinwater(exists as micelles); soluble in organicsolvent
5. Exist as aphospholipidbilayeratthe cell/organelle surface, i.e. cellmembrane
6. Mayhave small variable moleculesattached tothe phosphate 'head' e.g. choline
1. Insolubleinwater; soluble in organiccompounds
Some reproductive hormones.
2. Possess 4 interconnectedC rings
progesterone
3. Structurallylittle in common with otherlipids
(J)
4. e.g. cholesterol, vitamin D, steroid hormones
en
Q
Cl
0: CH,
yH)
co

CH ' 1 I
)...........
CH?H
CH,
testosterone
cJ
0'''-''''' '/
+ 3HzO
FUNCTION
1. HigherH:Oratlqcomparedto carbohydrates
good energystore(2xthatofcarbohydrates)
Hence, animals storemoreenergywith less
weightthan plants
enables animalstotravel aroundwith less
weight
2,Goodinsulatorofheat
used byanimalsto retain bodyheat
e.g,blubber, subcutaneousfat
3.Goodbarrierofions
allowssaltatoryconduction ofnerve
impulses
henceincreasetransmission ofimpulsegreatly
4, Protection:Abletoabsorb impact
cushionsvital organsforprotection
5, Lessdensethanwater
aquaticanimalscan staybuoyantin water
6,Releaseswaterasaby-productwhen oxidised
metabolicwateris ausefulsourceofwaterfor
desertanimals, orfordev, ofavian and retileeggs
1. Bilayersform continuoussheets
serve as membranesthatenclose
cell/organelles, allows compartmentalisation
2. Hydrophobiccore:selectivelypermeablemembrane
allows lipid-solublemoleculestopassthrough
readily
althoughwateris polar, itcan pass through
occasionallybecauseit is small and
weakin charge
regulates movementofions, polarmolecules
into and outofcell
3. Hydrophobicinteractionsbetween themolecules
self-sealing:will reseal quicklyifthey are
punctured ordisrupted
4-ring structure ofcholesterol (within membrane)
regulates/modulates membranefluidity
Atlowtemperature, preventphospholipids
from gettingtoo closetogetherand therefore
prevents solidification ofmembrane
athigh temperature, preventthe membrane
from being excessivelyfluidand unstable at
highertemperaturesthrough theirinteraction
with phospholipids
1.Structurallysimilarto fats and oils, onlythatthe long-chained fatty acids are linked to long-chained alcohols Insoluble
2. Insoluble in water cutin: coats surfaceofleavesto reduce waterloss
><
<tl
3. Chemicallyinert similarconceptwith insects
I/l
3
I/l
PROCEDURE
1. Place2cm3 oftestsolution in atesttube
:;og'
(l) :J
2. AddequalvolumeofBenedict'sreagent
c.(l)
c: c. 3. Shakethe mixture
Q. o
:J ~ 4. Heatitbyimmersingthetube in boilingwaterbathfor2minutes
<0 (';
5. Observethecontents ofthetube
(J)-I
c: (l)
<0 (J>
III ~
en Q
z
1. Ifanegative resultforBenedict'stest is obtained fortestsolution,
o
2. Boilequalvolumeoftestsolutionwith diluteHCI forabout 1minute
'?
to hydrolysedisaccharideto monosaccharides
~ - I
c: (l) 3. Coolthe contentsofthe tube
Q. ~
:J ..., 4. Neutralisethe contentswith sodium hydrogen/carbonatesolution
<0 0
(J)""'
because Benedict'sregentonlyworksin alkaline conditions
c
<0
5. Carryout Benedict'stestforreducing sugar
III
6. Record observations in the sameformatas thatforBenedict'stest
Ul
1. Add afewdrops ofpotassiumiodidesolutionto 1cm3of
0'[ testsolution (orapiece ofthetestspecimen)
S2 ~ 2. Observeanycolourchange
III -I
""' (l)
g . ~
1. Place 2cm3 oftestsolutionin atest-tube
2. Add equalvolume of5%NaOHsolution
O'OJ
..., c
3. Shakethe mixturewell
-0""'
""' (l)
o ~ 4. Add 1%coppersulphate solution, drop bydrop, shakingwell
(ii-l
_. (l) aftereach drop
:J (J>
(J> ~
5. Observe anycolourchange
m
1. Place 2cm3 ofabsoluteethanol in atest-tuibe
s:
III 2. Add 2cm3 of testsolution tothistest-tube
:J
...,0 2. Dissolve the contentsbyshakingvigorously
o -
""' m 3. Add equalvolume (i.e. 4cm3) ofcold water
C.3
u c: 4. Observe anycolourchange
CiiJi'
'" o
:J
-I
(l)
~
OBSERVATIONS
1. The contents ofthe test-tube remains ablue solution
2. A green pptforms in the contents ofthe test-tube
3.A yellowpptforms in thecontents ofthe test-tube
4. A brown pptforms in thecontents ofthe test-tube
5. A brick-red pptforms in the contents ofthe test-tube
1. The contents ofthe test-tube remains ablue solution
2. A green pptforms in the contents ofthe test-tube
3.A yellowpptforms in the contents ofthetest-tube
4. A brown pptforms in the contents ofthe test-tube
5. A brick-red pptforms in the contentsofthe test-tube
1. Themixtureturns blue-blackin colour
2. Themixture remainsyellowish-brown in colour
1.Themixtureturnsfrom bluetopurple/violet
2. Themixture remains blue in colour(because ofthe
coppersulphate solution)
1. The mixture turns aclearsolution
2.The mixtureturns acloudywhite suspension/an emulsion
is formed
CONCLUSIONS
1. No reducing sugars presentin the testsolution
2.A smallamountofreducing sugars is presentin the
a
~
testsolution
3. A moderateamountofreducing sugars is present in the
testsolution
4. A moderatelylarge amountofreducing sugars is
presentin the testsolution
5. A large amountofreducing sugars are presentin the
testsolution
1. Non reducing sugars absent in the test solution
2. A small amountofnon-reducing sugars is presentin the
testsolution
3. A moderateamountofnon-reducing sugarsis presentin
thetestsolution
4. A moderatelylarge amountof non-reducing sugars is
presentin the testsolution
5. A large amountofnon-reducing sugars are presentin the
testsolution
1. Starch is presentin the test solution
2. Starch is absentin the testsolution
1. Proteins are presentin thetestsolution
2. Proteins are absentin thetestsolution
1. Lipids are absentin the test solution
2. Lipids are presentin the testsolution