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@ARTICLE{Monkenbusch:11981,
author = {Monkenbusch, M. and Richter, D. and Biehl, R.},
title = {{O}bservation of protein domain motions by neutron
spectroscopy},
journal = {ChemPhysChem},
volume = {11},
issn = {1439-4235},
address = {Weinheim},
publisher = {Wiley-VCH Verl.},
reportid = {PreJuSER-11981},
pages = {1187 - 1194},
year = {2010},
note = {Record converted from VDB: 12.11.2012},
abstract = {High-resolution inelastic neutron scattering, which is
available with neutron spin-echo spectroscopy (NSE) is
introduced as a tool for the analysis of biomolecule
flexibility. Coherent scattering in a range where it is
sensitive to length scales of nanometers and covering a time
range from picoseconds to several 100 ns makes the motion of
larger subdomains within proteins visible. We show that and
how the internal domain motion within a protein in solution
can be measured. Comparison with displacement patterns from
normal mode analysis provides further insight into the
nature of the geometry of the motions that lead to the
observed dynamic signature. The NSE experiment on alcohol
dehydrogenase (ADH) is used as example to illustrate the
general principles of the method.},
keywords = {Alcohol Dehydrogenase: chemistry / Molecular Dynamics
Simulation / NAD: chemistry / Neutron Diffraction / Protein
Structure, Tertiary / NAD (NLM Chemicals) / Alcohol
Dehydrogenase (NLM Chemicals) / J (WoSType)},
cin = {IFF-4 / IFF-5 / Jülich Centre for Neutron Science JCNS
(JCNS) ; JCNS},
ddc = {540},
cid = {I:(DE-Juel1)VDB784 / I:(DE-Juel1)VDB785 /
I:(DE-Juel1)JCNS-20121112},
pnm = {BioSoft: Makromolekulare Systeme und biologische
Informationsverarbeitung / Großgeräte für die Forschung
mit Photonen, Neutronen und Ionen (PNI)},
pid = {G:(DE-Juel1)FUEK505 / G:(DE-Juel1)FUEK415},
shelfmark = {Chemistry, Physical / Physics, Atomic, Molecular $\&$
Chemical},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:19924753},
UT = {WOS:000277666900010},
doi = {10.1002/cphc.200900514},
url = {https://juser.fz-juelich.de/record/11981},
}