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• W1875724897 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." @default.
• W1875724897 created "2016-06-24" @default.
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• W1875724897 date "2015-08-21" @default.
• W1875724897 modified "2023-09-26" @default.
• W1875724897 title "Fast internal dynamics in alcohol dehydrogenase" @default.
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• W1875724897 doi "https://doi.org/10.1063/1.4928512" @default.
• W1875724897 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26298156" @default.
• W1875724897 hasPublicationYear "2015" @default.
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