Abstract
Apparently contradictory statements about the thermodynamics of aqueous protein solutions and of hydrophobic effect are quoted and discussed. Some credibility is found in the divergent points of view and it is pointed out that they focus attention on different aspects of the complicated conditions in aqueous solutions, some of which are more important than others for the stability of protein conformations.
The importance of characteristics of solvent water is emphasized, in particular (1) the strong mutual cohesion of water molecules, and (2) structural changes of water induced by (nonpolar) solute molecules. It is stressed that consideration of only one of these effects and an inexpedient choice of standard states are origins of confusion in the literature about aqueous systems. A simple approach to hydrophobic effects considering both of the above mentioned effects, is proposed.
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Hvidt, A., Westh, P. Different Views on the Stability of Protein Conformations and Hydrophobic Effects. Journal of Solution Chemistry 27, 395–402 (1998). https://doi.org/10.1023/A:1022696404041
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DOI: https://doi.org/10.1023/A:1022696404041