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@ARTICLE{Gaspar:8207,
author = {Gaspar, A.M. and Busch, S. and Appavou, M.-S. and
Haeussler, W. and Georgii, R. and Su, Y. and Doster, W.},
title = {{U}sing polarization analysis to separate the coherent and
incoherent scattering from protein samples},
journal = {Biochimica et biophysica acta},
volume = {1804},
issn = {0006-3002},
address = {Amsterdam [u.a.]},
publisher = {Elsevier},
reportid = {PreJuSER-8207},
pages = {76 - 82},
year = {2010},
note = {A. M. Gaspar acknowledges the support given by Fundacao
para Ciencia e Tecnologia in the form of a post-doc grant
SFRH/BDP/17571/2004. The project was further supported by a
grant of the Deutsche Forschungsgemeinschaft SFB 533.},
abstract = {Polarization analysis was used to separate experimentally
the coherent and spin-incoherent nuclear static scattering
functions, from a representative set of samples of interest
for protein studies. This method had so far limited
application in the study of amorphous materials, despite the
relevance of the information that it provides. It allows,
for instance, the experimental determination of the
structure factor of materials containing a significant
amount of hydrogen atoms, avoiding the contamination of
measurements by a non-negligible incoherent background.
Knowledge of the relative importance of the coherent and
incoherent terms at different Q-values is also a
pre-requisite for the interpretation of quasielastic neutron
scattering experiments, performed at instruments in which
the total dynamic scattering function is measured, such as
conventional time-of-flight and backscattering
spectrometers. Combining data from different instruments, it
was possible to cover a wide Q-range, from the small-angle
region (0.006<Q<0.04 A(-1)) to the wide-angle region (up to
approximately 2.35 A(-1)). Quantitative information was
obtained on the fraction of coherent to spin-incoherent
scattering from different protein samples: deuterated and
protonated protein powders at different hydration levels and
solutions of protonated proteins in D(2)O at different
concentrations. The results obtained are discussed in the
context of the validity of the assumptions generally made
when interpreting quasielastic neutron scattering
experiments performed without polarization analysis.},
keywords = {Deuterium Oxide: chemistry / Hemoglobins: chemistry /
Models, Chemical / Myoglobin: chemistry / Neutron
Diffraction: methods / Phycocyanin: chemistry / Proteins:
chemistry / Solutions / Water: chemistry / Hemoglobins (NLM
Chemicals) / Myoglobin (NLM Chemicals) / Proteins (NLM
Chemicals) / Solutions (NLM Chemicals) / Phycocyanin (NLM
Chemicals) / Water (NLM Chemicals) / Deuterium Oxide (NLM
Chemicals) / J (WoSType)},
cin = {IFF-4 / IFF-5 / Jülich Centre for Neutron Science JCNS
(JCNS) ; JCNS},
ddc = {570},
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},
experiment = {EXP:(DE-MLZ)DNS-20140101 / EXP:(DE-MLZ)MIRA-20140101 /
EXP:(DE-MLZ)RESEDA-20140101},
shelfmark = {Biochemistry $\&$ Molecular Biology / Biophysics},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:19595800},
UT = {WOS:000272765200012},
doi = {10.1016/j.bbapap.2009.06.024},
url = {https://juser.fz-juelich.de/record/8207},
}