Question

Explain the thermodynamics of protein folding including in your discussion how enthalpy and entropy drive protein folding and the relative strength of its change in free energy.

Answer 1

There is always free energy change and protein folding occurs spontaneously. The change in entropy is negative for a spontaneous process and when the protein folds, there is decrease in entropy as the protein are more ordered and organized. But also it is favored by enthalpy as the increase in protein folding leads to formation of hydrogen bonds between amino acids that are polar and water. Along with the hydrogen bonds, covalent and hydrophobic bonds are also formed which increase the enthalpy. In case of protein folding, the enthalpy increases due to formation of Vanderwaals interactions and electrostatic interactions which minimize the energy that is used in folding of the protein. Entropy is a process where it is the driving force.