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CYL120Inorganicandorganicchemistry:Conceptsandapplication,SemesterII(20112012)

InorganicChemistryTutorialSheet7(TutorialTeachers:Prof.A.J.EliasandDr.S.Nagendran)

Bio-Inorganic Chemistry
1. Indicate the basic structural differences between helix and pleated sheet structural motifs of
proteins.

2. Fromthegivensetofaminoacids,indicatepairsofaminoacid(s)whichcanhavea)disulfurbridges,b)
electrostaticattraction,c)hydrogenbondingbetweenresidues,andd)hydrophobicinteraction.
H
H 2N

H
COOH

H2 N

CH2

H
COOH

H2 N

CH2

COOH

H2 N

CH 2

C
HC

CH2

COOH
CH3

CH 2
N

CH2

CH 3
NH

CH2
NH 2

OH

H
H2 N

H
COOH

H 2N

H
COOH

CH 2

CH2

SH

COOH

H2 N

COOH

CH3

3. Drawexamplesofprostheticgroupsofbiomoleculeshavingcopperinatetrahedralenvironmentand
ironinanoctahedralenvironment

4. Canisolatedhememoleculesbeusedformakingdioxygencomplexes?Justifyyouranswer.

5. What is the oxidation state of the metal and nature of the dioxygen moiety in oxyhemoglobin? Give
evidencestosupportyouranswer.

6. Indicatewhetherthefollowingstatementsaretrueorfalse:
a. Hemoglobinisanexacttetramerofmyoglobinmolecule
b. Disulfurlinkagesbetweenproteinchainscanbeeasilybrokenandreformed

c. The role of a metal ion in the centre of a porphyrin unit is only to provide a site for ligand
coordinationandredoxactivity
d. Myoglobinhasaproteinchainwithismostlymadeofhelices

7. Give an equation indicating the catalytic function of carbonic anhydrase. In what way is carbonic
anhydraseactivityrelatedtofunctioningofhemoglobin?

8. Althoughhemeunitsofbothmyoglobinandoxymyoglobinarehavingunpairedelectronsonlyoneof
thisparamagnetic. Explain.

9. ExplainBohrEffect.

10. In what ways structural changes on oxygenation at the active site is different for hemoglobin in
comparisontomyoglobin.