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• W1966230467 abstract "We probe the effects of solute length scale, attractions, and hydrostatic pressure on hydrophobic hydration shells using extensive molecular simulations. The hydration shell compressibility and water fluctuations both display a nonmonotonic dependence on solute size, with a minimum near molecular solutes and enhanced fluctuations for larger ones. These results and calculations on proteins suggest that the hydration shells of unfolded proteins are more compressible than of folded ones contributing to pressure denaturation. More importantly, the nonmonotonicity implies a solute curvature-dependent pressure sensitivity for interactions between hydrophobic solutes." @default.
• W1966230467 created "2016-06-24" @default.
• W1966230467 creator A5003671262 @default.
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• W1966230467 date "2009-07-17" @default.
• W1966230467 modified "2023-09-23" @default.
• W1966230467 title "Quantifying Water Density Fluctuations and Compressibility of Hydration Shells of Hydrophobic Solutes and Proteins" @default.
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• W1966230467 doi "https://doi.org/10.1103/physrevlett.103.037803" @default.
• W1966230467 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19659321" @default.
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