Heat capacity and entropy changes in processes involving proteins.
Six possible sources of the large heat capacity and entropy changes frequently 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 estimating 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.
D002151:Calorimetry; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D006358:Hot Temperature; D009243:NAD; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins; D013816:Thermodynamics
D011506:Proteins; D009243:NAD; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases