971. For the unfolding reaction of Protein G, ΔH° =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

972. 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

973. 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

974. At the midpoint of a temperature transition curve,
A. half of the protein is denatured
B. Keq = 1.0 and ΔG = 0
C. [Native] = [Unfolded]
D. All of these

975. 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

976. 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

977. Since ΔG° = -RTlnK
A. a 10-fold increase in K decreases ΔG° by about 10-fold
B. a 10-fold decrease in K decreases ΔG° by about 2.3*RT
C. a 10-fold increase in K decreases ΔG° by about 2.3*RT
D. a 10-fold decrease in K increases ΔG° by about 10-fold

978. The correlation between free energy ΔG 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

979. 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

980. 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

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