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@ARTICLE{Biehl:541,
author = {Biehl, R. and Hoffmann, B. and Monkenbusch, M. and Falus,
P. and Préost, S. and Merkel, R. and Richter, D.},
title = {{D}irect {O}bservation of {C}orrelated {I}nterdomain
{M}otion in {A}lcohol {D}ehydrogenase},
journal = {Physical review letters},
volume = {101},
issn = {0031-9007},
address = {College Park, Md.},
publisher = {APS},
reportid = {PreJuSER-541},
pages = {138102-1 - 138102-4},
year = {2008},
note = {Record converted from VDB: 12.11.2012},
abstract = {Interdomain motions in proteins are essential to enable or
promote biochemical function. Neutron spinecho spectroscopy
is used to directly observe the domain dynamics of the
protein alcohol dehydrogenase. The collective motion of
domains as revealed by their coherent form factor relates to
the cleft opening dynamics between the binding and the
catalytic domains enabling binding and release of the
functional important cofactor. The cleft opening mode
hardens as a result of an overall stiffening of the domain
complex due to the binding of the cofactor.},
keywords = {J (WoSType)},
cin = {IBN-4 / IFF-5 / IFF-4 / Jülich Centre for Neutron Science
JCNS (JCNS) ; JCNS},
ddc = {550},
cid = {I:(DE-Juel1)VDB802 / I:(DE-Juel1)VDB785 /
I:(DE-Juel1)VDB784 / I:(DE-Juel1)JCNS-20121112},
pnm = {Kondensierte Materie / Großgeräte für die Forschung mit
Photonen, Neutronen und Ionen (PNI)},
pid = {G:(DE-Juel1)FUEK414 / G:(DE-Juel1)FUEK415},
shelfmark = {Physics, Multidisciplinary},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000259680600076},
doi = {10.1103/PhysRevLett.101.138102},
url = {https://juser.fz-juelich.de/record/541},
}