BICH 409 FINAL EXAM REVIEW (CUMULATIVE
MATERIAL) UPDATED ACTUAL QUESTIONS AND
CORRECT ANSWERS
Question:
1. Which reagent would be most useful in determining the
N-terminal residue of a polypeptide?
Answer:
phenylisothiocyanate
Question:
2. Which reagent will reduce disulfide bonds?
Answer:
beta-mercapto ethanol
Question:
3. What is the advantage of adding SDS to gel
electrophoresis?
Answer:
allows proteins to be separated on the basis of approximate mass
Question:
4. Which reagent is used to purify proteins by salt
fractionation?
Answer:
ammonium sulfate
Question:
5. Which reagent cleaves on the C-side of methionine
residues?
Answer:
cyanogen bromide
Question:
6. Gel filtration chromatography fractionates proteins based
on:
Answer:
molecular size
,Question:
7. The spatial arrangement of protein subunits is called:
Answer:
quaternary structure
Question:
8. The folded states of globular proteins in aqueous
solutions are stabilized mainly by:
Answer:
hydrophobic interactions
Question:
9. The slowest step of protein folding is:
Answer:
the conformational adjustments to optimize the orientation of the side chains
Question:
10. A peptide bond has partial __________
Answer:
bond character
Question:
11. In an alpha-helix, the hydrogen bonding interaction
involves which atoms or groups?
Answer:
the carbonyl C=O of residue number n, with the amide N-H residue of residue
number n+4
Question:
12. When the pH increases from 7.2 to 7.4, the oxygen affinity
of hemoglobin:
Answer:
increases
Question:
13. 2,3-bisphosphoglycerate is bound to hemoglobin
primarily through ______________
Answer:
electrostatic interactions
, Question:
14. In both myoglobin and hemoglobin, the role of the
proximal histidine is to:
Answer:
coordinate to the heme iron
Question:
15. When a histidine residue is brought into close proximity
to an aspartate residue the pKa of the histidine
_________________
Answer:
increases
Question:
16. When the pH decreases from 7.4 to 7.2, the oxygen
affinity of myoglobin _____________
Answer:
remains unchanged
Question:
17. The most important biological function of the distal
histidine of hemoglobin is to:
Answer:
decrease the affinity of the heme for carbon monoxide
Question:
18. If the pH decreases from 7.4 to 7.3, the p50 of
hemoglobin would:
Answer:
increase
Question:
19. The serine proteases are an example of what type of
reaction?
Answer:
Bi Bi ping pong reaction
Question:
20. Which enzyme accelerates reactions by covalent
catalysis?
Answer:
elastase
MATERIAL) UPDATED ACTUAL QUESTIONS AND
CORRECT ANSWERS
Question:
1. Which reagent would be most useful in determining the
N-terminal residue of a polypeptide?
Answer:
phenylisothiocyanate
Question:
2. Which reagent will reduce disulfide bonds?
Answer:
beta-mercapto ethanol
Question:
3. What is the advantage of adding SDS to gel
electrophoresis?
Answer:
allows proteins to be separated on the basis of approximate mass
Question:
4. Which reagent is used to purify proteins by salt
fractionation?
Answer:
ammonium sulfate
Question:
5. Which reagent cleaves on the C-side of methionine
residues?
Answer:
cyanogen bromide
Question:
6. Gel filtration chromatography fractionates proteins based
on:
Answer:
molecular size
,Question:
7. The spatial arrangement of protein subunits is called:
Answer:
quaternary structure
Question:
8. The folded states of globular proteins in aqueous
solutions are stabilized mainly by:
Answer:
hydrophobic interactions
Question:
9. The slowest step of protein folding is:
Answer:
the conformational adjustments to optimize the orientation of the side chains
Question:
10. A peptide bond has partial __________
Answer:
bond character
Question:
11. In an alpha-helix, the hydrogen bonding interaction
involves which atoms or groups?
Answer:
the carbonyl C=O of residue number n, with the amide N-H residue of residue
number n+4
Question:
12. When the pH increases from 7.2 to 7.4, the oxygen affinity
of hemoglobin:
Answer:
increases
Question:
13. 2,3-bisphosphoglycerate is bound to hemoglobin
primarily through ______________
Answer:
electrostatic interactions
, Question:
14. In both myoglobin and hemoglobin, the role of the
proximal histidine is to:
Answer:
coordinate to the heme iron
Question:
15. When a histidine residue is brought into close proximity
to an aspartate residue the pKa of the histidine
_________________
Answer:
increases
Question:
16. When the pH decreases from 7.4 to 7.2, the oxygen
affinity of myoglobin _____________
Answer:
remains unchanged
Question:
17. The most important biological function of the distal
histidine of hemoglobin is to:
Answer:
decrease the affinity of the heme for carbon monoxide
Question:
18. If the pH decreases from 7.4 to 7.3, the p50 of
hemoglobin would:
Answer:
increase
Question:
19. The serine proteases are an example of what type of
reaction?
Answer:
Bi Bi ping pong reaction
Question:
20. Which enzyme accelerates reactions by covalent
catalysis?
Answer:
elastase
