Hydration and heat stability effects on protein unfolding

The thermal denaturation of proteins has been elucidated in terms of the chain free energy and the hydration free energy. The thermodynamic quantities of protein unfolding are predicted from the three-dimensional structure and from the amino acid content in proteins. The dominant free energies in protein folding, cold denaturation and marginal stability are elucidated using those energies. The average thermodynamic quantities are derived for 20 amino acid residues. Good enthalpy-entropy correlations are observed for the denaturation process of proteins.