Skip to content
VuFind
  • 0 Items in e-Shelf (Full)
  • History
  • User Account
  • Logout
  • User Account
  • Help
    • English
    • Deutsch
  • Books & more
  • Articles & more
  • JuSER
Advanced
 
  • Literature Request
  • Cite this
  • Email this
  • Export
    • Export to RefWorks
    • Export to EndNoteWeb
    • Export to EndNote
    • Export to MARC
    • Export to MARCXML
    • Export to BibTeX
  • Favorites
  • Add to e-Shelf Remove from e-Shelf



QR Code
This title appears in the Scientific Report : 2015 

Fast internal dynamics in alcohol dehydrogenase

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...

More

Saved in:
Personal Name(s): Monkenbusch, M. (Corresponding author)
Stadler, A. / Biehl, R. / Ollivier, J. / Zamponi, M. / Richter, D.
Contributing Institute: Neutronenstreuung; JCNS-1
JCNS-FRM-II; JCNS-FRM-II
Neutronenstreuung; ICS-1
Published in: The journal of chemical physics, 143 (2015) 7, S. 075101 -
Imprint: Melville, NY American Institute of Physics 2015
PubMed ID: 26298156
DOI: 10.1063/1.4928512
Document Type: Journal Article
Research Program: Jülich Centre for Neutron Research (JCNS)
Soft Matter, Health and Life Sciences
Functional Macromolecules and Complexes
Subject (ZB):
Chemistry > 2
Biology > 0
Medicine > 1
Health and Life > 1
Health and Life > 0
Link: OpenAccess
OpenAccess
Publikationsportal JuSER
Please use the identifier: http://hdl.handle.net/2128/18992 in citations.
Please use the identifier: http://dx.doi.org/10.1063/1.4928512 in citations.

  • Description
  • Staff View

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.

  • Forschungszentrum Jülich
  • Central Library (ZB)
  • Powered by VuFind 6.1.1
Loading...