Fast internal dynamics in alcohol dehydrogenase

Monkenbusch, M.; Biehl, R.; Ollivier, J.; Richter, D.; Stadler, A.; Zamponi, M.

doi:10.1063/1.4928512

Journal Article

FZJ-2015-05653

Fast internal dynamics in alcohol dehydrogenase

Monkenbusch, M. (Corresponding author)FZJ* ; Stadler, A.FZJ* ; Biehl, R.FZJ* ; Ollivier, J. ; Zamponi, M.FZJ* ; Richter, D.FZJ*

2015
American Institute of Physics Melville, NY

The journal of chemical physics 143(7), 075101 - (2015) [10.1063/1.4928512]

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Please use a persistent id in citations: http://hdl.handle.net/2128/18992 doi:10.1063/1.4928512

Abstract: 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 D2O solvent. It is tempting to associate the fast internal process with solvent exposed amino acid residues with dangling side chains.

Keyword(s): Health and Life (1st) ; Health and Life (1st) ; Chemistry (2nd) ; Biology (2nd) ; Medicine (2nd)