Individual degrees of freedom and the solvation properties of water.
Using molecular dynamics simulations in conjunction with home-developed Split Integration Symplectic Method we effectively decouple individual degrees of freedom of water molecules and connect them to corresponding thermostats. In this way, we facilitate elucidation of structural, dynamical, spectral, and hydration properties of bulk water at any given combination of rotational, translational, and vibrational temperatures. Elevated rotational temperature of the water medium is found to severely hinder hydration of polar molecules, to affect hydration of ionic species in a nonmonotonous way and to somewhat improve hydration of nonpolar species. As proteins consist of charged, polar, and nonpolar amino-acid residues, the developed methodology is also applied to critically evaluate the hypothesis that the overall decrease in protein hydration and the change in the subtle balance between hydration of various types of amino-acid residues provide a plausible physical mechanism through which microwaves enhance aberrant protein folding and aggregation.
Laboratory for Molecular Modeling, National Institute of Chemistry, Hajdrihova 19, SI-1001 Ljubljana, Slovenia.
Urban
U
Bren
Dušanka
D
Janežič
D008872:Microwaves; D056004:Molecular Dynamics Simulation; D009038:Motion; D009356:Neon / Q000737:chemistry; D011188:Potassium / Q000737:chemistry; D012399:Rotation; D012997:Solvents / Q000737:chemistry*; D013696:Temperature; D014732:Vibration; D014867:Water / Q000737:chemistry*
D012997:Solvents; D014867:Water; D009356:Neon; D011188:Potassium