Many biological macromolecules undergo a transition called denaturation. Denaturation is a process whereby a structured, biological active molecule, called the native form, unfolds or becomes unstructured and biologically inactive. The equilibrium is:
nature(folded) <-----> denatured(unfolded)
For a protein at pH = 2, the enthalpy change associated with denaturation is deltaH° = 418.0 kJ mol-1 and the entropy change is deltaS° = 1.3 kJ K-1 mol-1 at T=298.15 K.
a. Calculate the Gibbs energy change for the denaturation of the protein at pH = 2 and T = 303 K. Assume the enthalpy and entropy are temperature independent between 298.15 and 303 K.
b. Calculate the equilibrium constant for the denaturation of protein at pH = 2 and T = 303 K.
c. Based on your answers for parts (a) and (b), is protein structurally stable at pH = 2 and T = 303 K?