TY  - JOUR
AU  - Monkenbusch, M.
AU  - Stadler, A.
AU  - Biehl, R.
AU  - Ollivier, J.
AU  - Zamponi, M.
AU  - Richter, D.
TI  - Fast internal dynamics in alcohol dehydrogenase
JO  - The journal of chemical physics
VL  - 143
IS  - 7
SN  - 1089-7690
CY  - Melville, NY
PB  - American Institute of Physics
M1  - FZJ-2015-05653
SP  - 075101 -
PY  - 2015
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000360440400051
C6  - pmid:26298156
DO  - DOI:10.1063/1.4928512
UR  - https://juser.fz-juelich.de/record/255491
ER  -