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@ARTICLE{Appavou:18195,
author = {Appavou, M-S. and Busch, S. and Doster, W. and Gaspar, A.
and Unruh, T.},
title = {{T}he influence of 2 kbar pressure on the global and
internal dynamics of human hemoglobin observed by
quasielastic neutron scattering},
journal = {European biophysics journal},
volume = {40},
issn = {0175-7571},
address = {Berlin},
publisher = {Springer},
reportid = {PreJuSER-18195},
pages = {705 - 714},
year = {2011},
note = {The research project was supported by a grant of the
Deutsche Forschungsgemeinschaft, SFB 533, TP B11, which is
gratefully acknowledged. We would like to acknowledge
particularly Joachim Dorbecker and Reinhold Funer who helped
to build the 2 kbar pressure cell and the platform for
TOFTOF. We would like to thank Jandal Ringe for his help on
TOFTOF during our experiments. The ANTARES team, especially
Martin Muhlbauer and Elbio Calzada, are thanked for allowing
us to use some beam time for neutronography measurements,
and to Robert Georgii for beamtime on MIRA to perform the
SANS characterization measurements. Finally, we would like
to thank Alan Soper for useful discussions.},
comment = {..},
booktitle = {..},
abstract = {Pressure is a ubiquitous physical parameter in life and is
commonly used in the life sciences to study new protein
folding pathways or association-dissociation phenomena. In
this paper, an investigation of the influence of pressure on
hemoglobin, a multimeric protein, at the picosecond time
scale is presented using time-of-flight neutron scattering.
The aim is to observe the influence of pressure on the
translational diffusion and internal motions of hemoglobin
in a concentrated solution and a possible dissociation of
the subunits as suggested by Pin et al. (Biochemistry
29:9194, 1990) using fluorescence spectroscopy. A new flat 2
kbar pressure cell made of an aluminum alloy has been used,
which allowed the effect of pressure to be studied with
minimum background contribution. Within this range of
pressure, the effect of this physical parameter on global
diffusion can be explained in terms of the change in the
water buffer viscosity and an oligomerization of hemoglobin
subunits, whereas the internal motions were less affected.},
keywords = {Diffusion / Hemoglobin Subunits: chemistry / Humans /
Motion / Neutron Diffraction: methods / Pressure / Protein
Conformation / Scattering, Radiation / Viscosity /
Hemoglobin Subunits (NLM Chemicals) / J (WoSType)},
cin = {ICS-1 / JCNS (München) ; Jülich Centre for Neutron
Science JCNS (München) ; JCNS-FRM-II / JCNS-1 / JCNS-2},
ddc = {570},
cid = {I:(DE-Juel1)ICS-1-20110106 /
I:(DE-Juel1)JCNS-FRM-II-20110218 /
I:(DE-Juel1)JCNS-1-20110106 / I:(DE-Juel1)JCNS-2-20110106},
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},
experiment = {EXP:(DE-MLZ)TOF-TOF-20140101},
shelfmark = {Biophysics},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:21340585},
UT = {WOS:000290331400001},
doi = {10.1007/s00249-011-0678-3},
url = {https://juser.fz-juelich.de/record/18195},
}