Protein hydration dynamics in aqueous solution

摘要: Water oxygen-17 and deuteron spin relaxation rates, measured as a function of resonance frequency, have been used to study the dynamics protein hydration in aqueous solutions ribonuclease A, lysozyme, myoglobin, trypsin serum albumin. The data conform picture dynamics, proposed on basis previous studies smaller proteins, where long-lived water molecules responsible for dispersion are identified with small number integral seen crystal structures. These molecules, residence times range 10–9–10–3 s, either buried internal cavities, trapped narrow clefts or coordinated metal ions. For traditional layer at surface, suggest an average time 10–50 ps, consistent high-resolution 1H spectroscopy computer simulations. also reveal some more specific features hydration, relating cavities that appear empty by crystallography, entrapment between structural domains large proteins subnanosecond 180° flips clusters.