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 at 298 K associated with denaturation is ΔH^o = 418.0 kJ mol⁻¹ and the entropy change at 298 K is ΔS^o = 1.30 kJ K⁻¹ mol⁻¹.

a. Calculate the Gibbs energy change for the denaturation of the protein at pH = 2 and T = 310.K.Assume the enthalpy and entropy are temperature-independent between 298.15 K and 310. K.

b. Calculate the equilibrium constant for the denaturation of the protein at pH = 2 and T = 310.K.

c. Based on your answer for parts (a) and (b), is the protein structurally stable at pH = 2 and T = 310.K?