1. 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. The 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. Express your answer with the appropriate units.
B) What must be the enthalpy change accompanying denaturation to allow the protein to be half-denatured at 50 °C?
2. What must be the enthalpy change accompanying denaturation to allow the protein to be half-denatured at 50 °C?