Does hydrophobic hydration destabilize protein native structures?
Water in the immediate vicinity of a non-polar solute has characteristically low entropy and high heat capacity at 25 degrees C. Common opinion has been that the insolubility of such species is caused by thermodynamic changes associated with the formation of these layers of abnormal water, 'hydrophobic hydration'. Recently, however, it has been proposed instead that hydrophobic hydration favors solution of hydrocarbons, or hydrocarbon sidechains, in water and therefore promotes protein unfolding. It is argued here that available data do not convincingly support this hypothesis.
Muller
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Department of Chemistry, Purdue University, West Lafayette, IN 47907.
D006860:Hydrogen Bonding; D008956:Models, Chemical; D011489:Protein Denaturation / Q000502:physiology*; D013816:Thermodynamics; D014867:Water / Q000737:chemistry
D014867:Water