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Biochemistry - Protein Stability

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
only at the ends of a-helices
only at the turns connecting p-strands
only on Pro residues
rarely
Answer: Option
Explanation:
No answer description is available. Let's discuss.
2.
For the unfolding reaction of Protein G, ΔH° =210.6 kJ/mol, this means that
unfolding is favored enthalpically
folding is favored enthalpically
the entropy is positive at all temperatures
the entropy is negative at all temperatures
Answer: Option
Explanation:
No answer description is available. Let's discuss.
3.
Attractive Vander Waals forces occur between
apolar molecules in the liquid state
any pair of nearby atoms
polar molecules in the solid state
only if other forces are less favorable
Answer: Option
Explanation:
No answer description is available. Let's discuss.
4.
Which of the following forces is the most favorable for protein folding?
Conformational entropy
Hydrophobic Interactions
Vander Waals interactions
Hydrogen bonds
Answer: Option
Explanation:
No answer description is available. Let's discuss.
5.
At the midpoint of a temperature transition curve,
half of the protein is denatured
Keq = 1.0 and ΔG = 0
[Native] = [Unfolded]
All of these
Answer: Option
Explanation:
No answer description is available. Let's discuss.
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