Many biological macromolecules undergo a transition called denaturation. Denaturation is a process whereby a structured, biologically active molecule, called the native form, unfolds or becomes unstructured and biologically inactive. The equilibrium is Native (folded) + denatured (unfolded) For a protein at pH = 2 the enthalpy change associated with denaturation is AH = 418.0 kJ/mol and the entropy change is AS = 1.3 kJ/K.mol both at 298.15K (a) Calculate the Gibbs free energy of denaturation of the protein at pH = 2 and T = 303K. Assume that enthalpy and entropy are temperature independent between 298.15K and 303K (b) Calculate the equilibrium constant for the denaturation of the protein at pH = 2 and T = 303K. (c) Based on your answers above, is the protein structurally stable at pH 2 and 303K?