

MCQOPTIONS
This section includes 29 Mcqs, each offering curated multiple-choice questions to sharpen your Biochemistry knowledge and support exam preparation. Choose a topic below to get started.
1. |
When = of myoglobin, the fractional saturation (Y) is about |
A. | 0.1 |
B. | 0.5 |
C. | 0.9 |
D. | 1.7 |
Answer» C. 0.9 | |
2. |
Hemoglobin has quaternary structure and is made up of |
A. | six polypeptide chains, two -chains and four -chains |
B. | two polypeptide chains, one -chains and one -chains |
C. | four polypeptide chains, two -chains and two -chains |
D. | five polypeptide chains, two -chains and three -chains |
Answer» D. five polypeptide chains, two -chains and three -chains | |
3. |
When pO2 = Kd of myoglobin, the fractional saturation (YO2) is about |
A. | 0.1 |
B. | 0.5 |
C. | 0.9 |
D. | 1.7 |
Answer» C. 0.9 | |
4. |
Peptides in the fully extended chain conformation |
A. | have Y = F = 180 |
B. | do not occur in nature |
C. | also have a cis geometry in their peptide bonds |
D. | are equivalent to the (3-sheet structure |
Answer» B. do not occur in nature | |
5. |
The oxygen in hemoglobin and myoglobin is bound to |
A. | the iron atom in the heme group |
B. | the nitrogen atoms on the heme |
C. | histidine residues in the protein |
D. | lysine residues in the protein |
Answer» B. the nitrogen atoms on the heme | |
6. |
An oil drop with a polar coat is a metaphor referring to the three dimensional structure of |
A. | fibrous proteins |
B. | collagen |
C. | globular proteins |
D. | silk protein |
Answer» D. silk protein | |
7. |
What was the first protein whose complete tertiary structure was determined? |
A. | Lysozyme |
B. | Myoglobin |
C. | Pancreatic ribonuclease |
D. | Pancreatic DNase |
Answer» C. Pancreatic ribonuclease | |
8. |
In the -pleated sheet |
A. | hydrogen bonds are formed between the peptide bonds |
B. | adjacent polypeptide chains can either be parallel or antiparallel |
C. | the polypeptide chain is fully extended |
D. | all of the above |
Answer» E. | |
9. |
The Ramachandran Plot illustrates the fact that |
A. | the peptide bond is planar |
B. | the F & Y angles can assume any value in a peptide |
C. | the F & Y angles can assume only a single value in a protein |
D. | the F & Y angles can assume approximately three different values |
Answer» E. | |
10. |
The resonance structures that can be drawn for the peptide bond indicate that the peptide bond |
A. | is stronger than an ordinary single bond |
B. | has partial double bond character |
C. | both (a) and (b) |
D. | is still not completely understood |
Answer» D. is still not completely understood | |
11. |
The major element of secondary structure in myoglobin and hemoglobin is |
A. | the P-strand |
B. | the a-helix |
C. | the reverse turn |
D. | All of these |
Answer» C. the reverse turn | |
12. |
The same peptide, Val-Lys-Glu-Met-Ser-Trp-Arg-Ala. was digested with chymotrypsin to produce |
A. | Val-Lys + Glu-Met-Ser + Trp-Arg-Ala. |
B. | Val-Lys-Glu-Met-Ser-Trp + Arg-Ala. |
C. | Val-Lys-Glu-Met-Ser + Trp-Arg-Ala. |
D. | Val-Lys-Glu-Met + Ser-Trp-Arg-Ala. |
Answer» C. Val-Lys-Glu-Met-Ser + Trp-Arg-Ala. | |
13. |
Which of the three subunits of the G proteins binds GDP and GTP? |
A. | Alpha |
B. | Beta |
C. | Gamma |
D. | Delta |
Answer» B. Beta | |
14. |
Disulfide bonds most often stabilize the native structure of |
A. | extracellular proteins |
B. | dimeric proteins |
C. | hydrophobic proteins |
D. | intracellular proteins |
Answer» B. dimeric proteins | |
15. |
What is the effect of a decrease in pH on hemoglobin oxygen affinity? |
A. | Decrease in oxygen affinity |
B. | Increase in oxygen affinity |
C. | No effect on oxygen affinity |
D. | Increase affinity in muscle cell otherwise decrease |
Answer» B. Increase in oxygen affinity | |
16. |
What is the proportion of glycine residues in collagenous regions? |
A. | One-fourth |
B. | One-third |
C. | Half |
D. | One-tenth |
Answer» C. Half | |
17. |
Which hemoglobin chain replaces the beta chain in embryonic hemoglobulin? |
A. | Delta |
B. | Epsilon |
C. | Gamma |
D. | Alfa |
Answer» C. Gamma | |
18. |
Secondary structure in protein refers to |
A. | linear sequence of amino acids joined together by peptide bond |
B. | three dimensional arrangement of all amino acids in polypeptide chain |
C. | regular folding of regions of the polypeptide chain |
D. | protein made up of more than one polypeptide chain |
Answer» D. protein made up of more than one polypeptide chain | |
19. |
Heme is the binding pocket of myoglobin and hemoglobin and is composed of |
A. | negatively charged residues |
B. | polar residues |
C. | hydrophobic residues |
D. | positively charged residues |
Answer» D. positively charged residues | |
20. |
Hydrogen bonds in a-helices are |
A. | more numerous than Vander Waals interactions |
B. | not present at Phe residues |
C. | analogous to the steps in a spiral staircase |
D. | roughly parallel to the helix axis |
Answer» E. | |
21. |
Which of the following is an example of tertiary structure in a protein? |
A. | A multimeric protein |
B. | An a-helix |
C. | A P-pleated sheet |
D. | A globular domain |
Answer» E. | |
22. |
The peptide, Val-Lys-Glu-Met-Ser-Trp-Arg-Ala, was digested with cyanogen bromide (CNBr) to produce: |
A. | Val-Lys + Glu-Met-Ser + Trp-Arg-Ala |
B. | Val-Lys-Glu-Met-Ser-Trp + Arg-Ala |
C. | Val-Lys-Glu-Met + Ser-Trp-Arg-Ala |
D. | Val-Lys-Glu + Met-Ser-Trp-Arg-Ala |
Answer» D. Val-Lys-Glu + Met-Ser-Trp-Arg-Ala | |
23. |
The peptide bond in proteins is |
A. | only found between proline residues |
B. | usually cis unless proline is the next amino acid |
C. | usually trans unless proline is the next amino acid |
D. | is planar because of steric hinderance |
Answer» D. is planar because of steric hinderance | |
24. |
The different orders of protein structure are determined by all of the following bond types except |
A. | peptide bonds |
B. | phospho-diester bonds |
C. | disulfide bridges |
D. | hydrogen bonds |
Answer» C. disulfide bridges | |
25. |
In deoxy hemoglobin (Hb), the Fe (II) is coordinated to |
A. | four nitrogens of heme, the proximal His, and a water molecule |
B. | four nitrogens of heme and to a water molecule |
C. | two nitrogens of heme and to three His residues in Hb |
D. | two nitrogens of heme and to three water molecules |
Answer» B. four nitrogens of heme and to a water molecule | |
26. |
In -pleated sheet structures neighbouring |
A. | chains lie in a flat plane |
B. | neighboring residues are hydrogen bonded |
C. | neighboring chains are connected by a-helices |
D. | neighboring chains are hydrogen bonded |
Answer» E. | |
27. |
The nature of peptide bond can be best explained as |
A. | partial double bond |
B. | truly double bond |
C. | Hydrogen bond |
D. | Van der waals force |
Answer» B. truly double bond | |
28. |
The oxygen binding curves of hemoglobin and myoglobin |
A. | allow maximum transfer of oxygen to the tissues |
B. | are a consequence of the quaternary structure of hemoglobin |
C. | both (a) and (b) |
D. | are identical |
Answer» D. are identical | |
29. |
If the F and Y angles of each peptide unit in a protein are known, which of the following may also be determined? |
A. | Complete secondary structure |
B. | Complete tertiary structure |
C. | Complete quaternary structure |
D. | Thermodynamic stability |
Answer» B. Complete tertiary structure | |