Question

1. In chapter 2, you learned that a polypeptide in solution usually folds spontaneously into its proper three-dimensional shape. The driving force for this folding is the tendency to achieve the most favored thermodynamic conformation. A folded polypeptide can be induced to unfold (i.e. will undergo denaturation) if the solution is heated or made acidic or alkaline. The denatured polypeptide is a random structure, with many possible conformations.

a. What is the sign of ∆G for the folding process? What about for the unfolding (denaturation) process? How do you know?

b. What is the sign for ∆S for the folding process? What about for the unfolding (denaturation) process? How do you know?

c. Will the contribution of ∆S to the free energy change be positive or negative?

d. What are the main kinds of bonds and interactions that must be broken or disrupted if a folded polypeptide is to be unfolded? Why do heat and extremes of pH cause unfolding?

Answer 1

Answer:

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