The major difference between a protein molecule in its native state and in its denatured state lies in the number of conformations available. To a first approximation, the native, folded state can be thought to have one conformation. Te unfolded state can be estimated to have three possible orientations about each bond between residues.
a. For a protein of 100 residues, estimate the entropy change per mole upon denaturation.
b. What must be the enthalpy change accompanying denaturation to allow the protein to be half-denatured at 50 °C?
c. Will the fraction denatured increase or decrease with increasing temperature?