Consider a small protein containing 101 amino acid residues. The protein would have 100 peptide bonds about which rotation can occur. Assume three orientations are possible about each of these bonds. (a) How many random-coil conformations will be possible for this protein (b) Estimate the conformational entropy change on folding 1 mole of this protein into a native structure with only one conformation (c) If the protein folds entirely into alpha-helix with H-bonds as the only source of enthalpy of stabilization, and each mole of H-bonds contribute -5 kJ/mol to the enthalpy, estimate ΔHfolding. Note that you can not form 4 H-bonds at one end. (d) From (b) and (c), estimate ΔGfolding for this protein at 298 K. Is the folded form stable at 298 K? (biochemistry)