Heat capacity and entropy changes in processes involving proteins.

Abstract

Six possible sources of the large heat capacity and entrophy changes frequency observed for processes involving proteins are identified. Of these the conformational, hydrophobic and vibrational effects seem likely to be of greatest importance. A method is proposed for estimting the magnitudes of the hydrophobic and vibrational contributions. Application of this method to several protein processes appears to achieve significant clarification of previously confusing and apparently contradictory data.