title: Dynamical transition, hydrophobic interface, and the temperature dependence of electrostatic fluctuations in proteins.
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 approximately 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.
authors.affiliation: Center for Biological Physics, Arizona State University, P.O. Box 871604, Tempe, Arizona 85287-1604, USA.
authors.forename: David N
authors.initials: DN
authors.lastname: Lebard
authors.forename: Dmitry V
authors.initials: DV
authors.lastname: Matyushov
mesh_terms: D055592:Biophysical Phenomena; D057927:Hydrophobic and Hydrophilic Interactions; D008956:Models, Chemical; D010970:Plastocyanin / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D055672:Static Electricity; D013696:Temperature; D013816:Thermodynamics; D014867:Water
chemical_list: D011506:Proteins; D014867:Water; D010970:Plastocyanin