Quantifying water density fluctuations and compressibility of hydration shells of hydrophobic solutes and proteins

Sapna Sarupria, Shekhar Garde

Research output: Contribution to journalArticlepeer-review

145 Scopus citations

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.

Original languageEnglish (US)
Article number037803
JournalPhysical review letters
Volume103
Issue number3
DOIs
StatePublished - Aug 6 2009
Externally publishedYes

Fingerprint

Dive into the research topics of 'Quantifying water density fluctuations and compressibility of hydration shells of hydrophobic solutes and proteins'. Together they form a unique fingerprint.

Cite this