Role of Protein-Water Hydrogen Bond Dynamics in the Protein Dynamical Transition

M. Tarek; D. J. Tobias

doi:10.1103/PhysRevLett.88.138101

Role of Protein-Water Hydrogen Bond Dynamics in the Protein Dynamical Transition

M. Tarek and D. J. Tobias

Phys. Rev. Lett. 88, 138101 – Published 14 March 2002

Abstract

The role of water in protein dynamics has been investigated using molecular dynamics simulations of crystals and a dehydrated powder. On the $100 ps$ time scale, the anharmonic and diffusive motions involved in the protein structural relaxation are correlated with the protein-water hydrogen bond dynamics. The complete structural relaxation of the protein requires relaxation of the hydrogen bond network via solvent translational displacement. Inhibiting the solvent translational mobility, and therefore the protein-water hydrogen bond dynamics, has an effect on the protein relaxation similar to dehydration.

Received 14 September 2001

DOI:https://doi.org/10.1103/PhysRevLett.88.138101

Authors & Affiliations

M. Tarek^1,2 and D. J. Tobias³

¹NIST Center for Neutron Research, National Institute of Standards and Technology, Gaithersburg, Maryland 20899-8562
²Chemistry Department, University of Pennsylvania, Philadelphia, Pennsylvania 19103-6323
³Department of Chemistry and Institute for Surface and Interface Science, University of California, Irvine, California 92697-2025