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MCQs

Total Questions : 26 | Page 3 of 3 pages
Question 21. . Buried hydrophobic side chains in a globular protein fit into a hole formed by the side chains of
  1.    1-3 other amino acids
  2.    5-7 other amino acids
  3.    9-12 other amino acids
  4.    13-15 other amino acids
 Discuss Question
Answer: Option B. -> 5-7 other amino acids
Question 22. . If the egg white protein, ovalbumin, is denatured in a hard-boiled egg, then which of the following is least affected?
  1.    The primary structure of ovalbumin
  2.    The secondary structure of ovalbumin
  3.    The tertiary structure of ovalbumin
  4.    The quaternary structure of ovalbumin
 Discuss Question
Answer: Option A. -> The primary structure of ovalbumin
Question 23. . Since ΔG° = -RTlnK
  1.    a 10-fold increase in K decreases ΔG° by about 10-fold
  2.    a 10-fold decrease in K decreases ΔG° by about 2.3*RT
  3.    a 10-fold increase in K decreases ΔG° by about 2.3*RT
  4.    a 10-fold decrease in K increases ΔG° by about 10-fold
 Discuss Question
Answer: Option C. -> a 10-fold increase in K decreases ΔG° by about 2.3*RT
Question 24. . Buried hydrophobic side chains in a globular protein fit into a hole formed by the side chains of
  1.    1-3 other amino acids
  2.    5-7 other amino acids
  3.    9-12 other amino acids
  4.    13-15 other amino acids
 Discuss Question
Answer: Option B. -> 5-7 other amino acids
Question 25. . If the egg white protein, ovalbumin, is denatured in a hard-boiled egg, then which of the following is least affected?
  1.    The primary structure of ovalbumin
  2.    The secondary structure of ovalbumin
  3.    The tertiary structure of ovalbumin
  4.    The quaternary structure of ovalbumin
 Discuss Question
Answer: Option A. -> The primary structure of ovalbumin
Question 26. . The correlation between free energy ΔG transfer between the aqueous/organic phases and the surface area of amino acid residues
  1.    reflects the reduction in solvent-accessible area during protein folding
  2.    is only meaningful for the polar amino acids
  3.    ignores the important contribution of the peptide bond
  4.    is similar to effects seen with SDS denaturation
 Discuss Question
Answer: Option A. -> reflects the reduction in solvent-accessible area during protein folding

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