Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
7842346 | Journal of Molecular Liquids | 2018 | 6 Pages |
Abstract
Cold denaturation is an intriguing phenomenon that deserves special attention because its rationalization is surely linked to a deeper understanding of the molecular determinants of the marginal stability of small globular proteins dissolved in water and aqueous solutions. It is here reviewed and discussed a theoretical approach that has offered a reliable explanation for the occurrence of both cold and hot denaturations. A cornerstone of the approach is the recognition of the role played by the density of water and its temperature-dependence that are largely determined by the special energetic and geometric features of H-bonds. In fact, the density of water determines the magnitude of the solvent-excluded volume effect, which is a main ingredient of the hydrophobic effect. The relationship between density and solvent-excluded volume effect establishes a strong connection between the physico-chemical properties of water and the conformational stability of small globular proteins.
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Authors
Antonio Grimaldi, Giuseppe Graziano,