Biochemistry - Protein Stability

Why Biochemistry Protein Stability?

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Exercise :: Protein Stability - Section 1

  • Protein Stability - Section 1
1. 

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: Option D

Explanation:

No answer description available for this question. Let us discuss.

2. 

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

Answer: Option B

Explanation:

No answer description available for this question. Let us discuss.

3. 

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: Option B

Explanation:

No answer description available for this question. Let us discuss.

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: Option B

Explanation:

No answer description available for this question. Let us discuss.

5. 

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

Answer: Option D

Explanation:

No answer description available for this question. Let us discuss.