MCQOPTIONS
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MCQOPTIONS
This section includes 10 Mcqs, each offering curated multiple-choice questions to sharpen your Biochemistry knowledge and support exam preparation. Choose a topic below to get started.
| 1. |
Attractive Vander Waals forces occur between |
| A. | apolar molecules in the liquid state |
| B. | any pair of nearby atoms |
| C. | polar molecules in the solid state |
| D. | only if other forces are less favorable |
| Answer» C. polar molecules in the solid state | |
| 2. |
Unpaired H-bond donors and acceptors are found in the hydrophobic core of a protein |
| A. | only at the ends of a-helices |
| B. | only at the turns connecting p-strands |
| C. | only on Pro residues |
| D. | rarely |
| Answer» E. | |
| 3. |
For the unfolding reaction of Protein G, H =210.6 kJ/mol, this means that |
| A. | unfolding is favored enthalpically |
| B. | folding is favored enthalpically |
| C. | the entropy is positive at all temperatures |
| D. | the entropy is negative at all temperatures |
| Answer» C. the entropy is positive at all temperatures | |
| 4. |
Which of the following forces is the most favorable for protein folding? |
| A. | Conformational entropy |
| B. | Hydrophobic Interactions |
| C. | Vander Waals interactions |
| D. | Hydrogen bonds |
| Answer» C. Vander Waals interactions | |
| 5. |
If the egg white protein, ovalbumin, is denatured in a hard-boiled egg, then which of the following is least affected? |
| A. | The primary structure of ovalbumin |
| B. | The secondary structure of ovalbumin |
| C. | The tertiary structure of ovalbumin |
| D. | The quaternary structure of ovalbumin |
| Answer» B. The secondary structure of ovalbumin | |
| 6. |
Since G = -RTlnK |
| A. | a 10-fold increase in K decreases G by about 10-fold |
| B. | a 10-fold decrease in K decreases G by about 2.3*RT |
| C. | a 10-fold increase in K decreases G by about 2.3*RT |
| D. | a 10-fold decrease in K increases G by about 10-fold |
| Answer» D. a 10-fold decrease in K increases G by about 10-fold | |
| 7. |
Buried hydrophobic side chains in a globular protein fit into a hole formed by the side chains of |
| A. | 1-3 other amino acids |
| B. | 5-7 other amino acids |
| C. | 9-12 other amino acids |
| D. | 13-15 other amino acids |
| Answer» C. 9-12 other amino acids | |
| 8. |
Which of the following is the most correct? |
| A. | Charged amino acids are never buried in the interior of a protein |
| B. | Charged amino acids are seldom buried in the interior of a protein |
| C. | All hydrophobic amino acids are buried when a protein folds |
| D. | Tyrosine is only found in the interior of proteins |
| Answer» C. All hydrophobic amino acids are buried when a protein folds | |
| 9. |
Which of the following forces is the most unfavorable for protein folding? |
| A. | Conformational entropy |
| B. | Hydrophobic interactions |
| C. | Vander Waals interactions |
| D. | Electrostatic interactions |
| Answer» B. Hydrophobic interactions | |
| 10. |
The correlation between free energy G transfer between the aqueous/organic phases and the surface area of amino acid residues |
| A. | reflects the reduction in solvent-accessible area during protein folding |
| B. | is only meaningful for the polar amino acids |
| C. | ignores the important contribution of the peptide bond |
| D. | is similar to effects seen with SDS denaturation |
| Answer» B. is only meaningful for the polar amino acids | |