The Role of Solvent in the Protein Dynamical Transition

Abstract

Experimental and computer simulation studies have revealed the presence of a transition in the dynamics of hydrated proteins around 220 K. This transition has been compared with that of a glass phase transition. It manifests itself by a nonlinear behavior in the temperature dependence of the average atomic mean-square displacements and involves an increase of the amplitude of protein dynamics. This increase in flexibility has been correlated with the onset of protein activity. In this thesis, the mechanisms behind the protein dynamical transition are explored using molecular dynamics simulations and neutron scattering experiments.