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@ARTICLE{Zhang:19773,
author = {Zhang, F. and Roosen-Runge, F. and Skoda, M.W.A. and
Jacobs, R.M.J. and Wolf, M. and Callow, P. and Frielinghaus,
H. and Pipich, V. and Prévost, S. and Schreiber, F.},
title = {{H}ydration and interactions in protein solutions
containing concentrated electrolytes studied by small-angle
scattering},
journal = {Physical Chemistry Chemical Physics},
volume = {14},
issn = {1463-9076},
address = {Cambridge},
publisher = {RSC Publ.},
reportid = {PreJuSER-19773},
pages = {2483 - 2493},
year = {2012},
note = {We gratefully acknowledge financial support from Deutsche
Forschungsgemeinschaft (DFG) and the beam time allocation
from ESRF, ILL, JCNS and Helmholtz-Center Berlin (BENSC).
The beam time on V4 at the Helmholtz Zentrum Berlin has been
supported by the European Commission under the 6th Framework
Program through the Key Action: Strengthening the European
Research Area, Research Infrastructures. Contract No.
RII3-CT-2003-505925 (NMI3).},
abstract = {During protein crystallization and purification, proteins
are commonly found in concentrated salt solutions. The exact
interplay of the hydration shell, the salt ions, and
protein-protein interactions under these conditions is far
from being understood on a fundamental level, despite the
obvious practical relevance. We have studied a model
globular protein (bovine serum albumin, BSA) in concentrated
salt solutions by small-angle neutron scattering (SANS). The
data are also compared to previous studies using SAXS. The
SANS results for dilute protein solutions give an averaged
volume of BSA of 91,700 Å(3), which is about $37\%$
smaller than that determined by SAXS. The difference in
volume corresponds to the contribution of a hydration shell
with a hydration level of 0.30 g g(-1) protein. The forward
intensity I(0) determined from Guinier analysis is used to
determine the second virial coefficient, A(2), which
describes the overall protein interactions in solution. It
is found that A(2) follows the reverse order of the
Hofmeister series, i.e. (NH(4))(2)SO(4) < Na(2)SO(4) < NaOAc
< NaCl < NaNO(3) < NaSCN. The dimensionless second virial
coefficient B(2), corrected for the particle volume and
molecular weight, has been calculated using different
approaches, and shows that B(2) with corrections for
hydration and the non-spherical shape of the protein
describes the interactions better than those determined from
the bare protein. SANS data are further analyzed in the full
q-range using liquid theoretical approaches, which gives
results consistent with the A(2) analysis and the
experimental structure factor.},
keywords = {Animals / Cattle / Electrolytes: chemistry / Neutron
Diffraction / Osmolar Concentration / Protein Interaction
Mapping / Salts: chemistry / Scattering, Small Angle / Serum
Albumin, Bovine: chemistry / X-Ray Diffraction /
Electrolytes (NLM Chemicals) / Salts (NLM Chemicals) / Serum
Albumin, Bovine (NLM Chemicals) / J (WoSType)},
cin = {ICS-1 / JCNS (München) ; Jülich Centre for Neutron
Science JCNS (München) ; JCNS-FRM-II / JCNS-1},
ddc = {540},
cid = {I:(DE-Juel1)ICS-1-20110106 /
I:(DE-Juel1)JCNS-FRM-II-20110218 /
I:(DE-Juel1)JCNS-1-20110106},
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)KWS2-20140101},
shelfmark = {Chemistry, Physical / Physics, Atomic, Molecular $\&$
Chemical},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:22249363},
UT = {WOS:000299505400046},
doi = {10.1039/c2cp23460b},
url = {https://juser.fz-juelich.de/record/19773},
}