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. What must be the sign of ∆S for the change: native → denatured?
b. How will the contribution of ∆S for native → denatured affect the favorability of the process? What apparent requirement does this impose on ∆ H if proteins are to be stable structures?