DISTRIBUTION FUNCTION IMPLIED DYNAMICS VERSUS RESIDENCE TIMES AND CORRELATIONS - SOLVATION SHELLS OF MYOGLOBIN

The dynamics of water at the protein-solvent interface is investigated through the analysis of a molecular dynamics simulation of metmyoglob in in explicit aqueous environment. Distribution implied dynamics, har monic and quasiharmonic, are compared with the simulated macroscopic d ynamics. The distinction between distinguishable solvent molecules and hydration sites developed in the previous paper is used. The simulate d hydration region within 7 Angstrom from the protein surface is analy zed using a set of 551 hydration sites characterized by occupancy weig hts and temperature B-factors determined from the simulation trajector y. The precision of the isotropic harmonic and anisotropic harmonic mo dels for the description of proximal solvent fluctuations is examined. Residence times and dipole reorientation times of water around the pr otein surface are compared with NMR and ESR results. A correlation bet ween diffraction experiment quantities such as the occupancy weights a nd temperature factors and the residence and correlation times resulti ng from magnetic resonance experiments is found via comparison with si mulation. (C) 1994 Wiley-Liss, Inc.