Chapter 3, Problem 7P

Assume that some protein molecule, in its folded native state, has one favored conformation. But when it is denatured, it becomes a “random coil,” with many possible conformations.
a. If we only consider the entropy for the protein, what must be the sign of $\Delta$ S for the charge native $\to$ denatured? (Note: As suggested in the next problem, this does not include solvent effects, which also make contributions to $\Delta$ S.)
b. How will the contribution of $\Delta$ S for native $\to$ denatured affect the favorability of the process? What apparent requirement does this impose on $\Delta$ H if proteins are to be stable structures?