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Title: Fast internal dynamics in alcohol dehydrogenase

Large-scale domain motions in alcohol dehydrogenase (ADH) have been observed previously by neutron spin-echo spectroscopy (NSE). We have extended the investigation on the dynamics of ADH in solution by using high-resolution neutron time-of-flight (TOF) and neutron backscattering (BS) spectroscopy in the incoherent scattering range. The observed hydrogen dynamics were interpreted in terms of three mobility classes, which allowed a simultaneous description of the measured TOF and BS spectra. In addition to the slow global protein diffusion and domain motions observed by NSE, a fast internal process could be identified. Around one third of the protons in ADH participate in the fast localized diffusive motion. The diffusion coefficient of the fast internal motions is around two third of the value of the surrounding D{sub 2}O solvent. It is tempting to associate the fast internal process with solvent exposed amino acid residues with dangling side chains.
Authors:
; ; ;  [1] ;  [2] ;  [3]
  1. Jülich Centre for Neutron Science JCNS and Institute for Complex Systems ICS, Forschungszentrum Jülich GmbH, 52425 Jülich (Germany)
  2. Institut Laue-Langevin, CS 20156, 38042 Grenoble (France)
  3. Jülich Centre for Neutron Science JCNS, Forschungszentrum Jülich GmbH, Outstation at MLZ, Lichtenbergstraße 1, 85747 Garching (Germany)
Publication Date:
OSTI Identifier:
22493556
Resource Type:
Journal Article
Resource Relation:
Journal Name: Journal of Chemical Physics; Journal Volume: 143; Journal Issue: 7; Other Information: (c) 2015 AIP Publishing LLC; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY; ALCOHOL DEHYDROGENASE; AMINO ACIDS; BACKSCATTERING; DIFFUSION; HEAVY WATER; HYDROGEN; INCOHERENT SCATTERING; MOBILITY; NEUTRON SPECTROSCOPY; PROTONS; RESIDUES; SOLVENTS; SPIN ECHO; TIME-OF-FLIGHT METHOD