Dynamical transition, hydrophobic interface, and the temperature dependence of electrostatic fluctuations in proteins

David N. Lebard, Dmitry Matyushov

Research output: Contribution to journalArticle

19 Scopus citations

Abstract

Molecular dynamics simulations have revealed a dramatic increase, with increasing temperature, of the amplitude of electrostatic fluctuations caused by water at the active site of metalloprotein plastocyanin. The increased breadth of electrostatic fluctuations, expressed in terms of the reorganization energy of changing the redox state of the protein, is related to the formation of the hydrophobic protein-water interface, allowing large-amplitude collective fluctuations of the water density in the protein's first solvation shell. On top of the monotonic increase of the reorganization energy with increasing temperature, we have observed a spike at 220 K also accompanied by a significant slowing of the exponential collective Stokes shift dynamics. In contrast to the local density fluctuations of the hydration-shell waters, these spikes might be related to the global property of the water solvent crossing the Widom line or undergoing a weak first-order transition.

Original languageEnglish (US)
Article number061901
JournalPhysical Review E - Statistical, Nonlinear, and Soft Matter Physics
Volume78
Issue number6
DOIs
StatePublished - Dec 1 2008

ASJC Scopus subject areas

  • Statistical and Nonlinear Physics
  • Statistics and Probability
  • Condensed Matter Physics

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