Protein aggregation reactions: surface free energy model.
The energetics of protein reactions can be evaluated in terms of the surface free-energy model, an approach that estimates changes in the surface free energy of proteins from changes in the area and the charge density of the protein-water interface. This approach has given insight into the reactions of proteins in solution as well as in membranes (receptors and voltage-gated channels). The model highlights the importance of pH and thermal changes in aggregation reactions. It also enables a correct interpretation of the Hill equation describing co-operative reactions, since the Hill coefficient is related to a Gibbs surface excess that varies with the degree of reaction.
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Department of Physiology and Cellular Biophysics, Columbia University, College of Physicians & Surgeons, New York, NY 10032.
D055598:Chemical Phenomena; D002627:Chemistry, Physical; D006863:Hydrogen-Ion Concentration; D008433:Mathematics; D008956:Models, Chemical; D011506:Proteins / Q000737:chemistry*; D014867:Water / Q000737:chemistry
D011506:Proteins; D014867:Water