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@ARTICLE{Ortore:57916,
author = {Ortore, M. G. and Spinozzi, F. and Carsughi, F. and
Mariani, P. and Bonetti, M. and Onori, G.},
title = {{H}igh pressure small-angle scattering study of the
aggregation state of beta-lactoglobulin in water and in
water/ethylene-glycol solutions},
journal = {Chemical physics letters},
volume = {418},
issn = {0009-2614},
address = {Amsterdam [u.a.]},
publisher = {Elsevier},
reportid = {PreJuSER-57916},
year = {2006},
note = {Record converted from VDB: 12.11.2012},
abstract = {High-pressure SANS experiments have been performed on
acidic dilute solutions of the dimeric protein
P-lactoglobulin. To evidence the solvent effect on the
protein stability during compression, two different
solvents, D2O and a $50\%$ w/w mixture of water and
ethyleneglycol have been considered. Data confirm that
pressure induces dissociation in both solvents, even if
P-lactoglobulin shows an higher stability in $50\%$
ethylene-glycol. An original global fitting procedure has
been used to derive the thermodynamic parameters that
describe the dissociation equilibrium. As a result, the role
of the solvent in protein dissociation has been observed to
reflect on volume and compressibility changes. (c) 2005
Elsevier B.V. All rights reserved.},
keywords = {J (WoSType)},
cin = {IFF-INS},
ddc = {540},
cid = {I:(DE-Juel1)VDB341},
pnm = {Kondensierte Materie / Großgeräte für die Forschung mit
Photonen, Neutronen und Ionen (PNI)},
pid = {G:(DE-Juel1)FUEK414 / G:(DE-Juel1)FUEK415},
shelfmark = {Chemistry, Physical / Physics, Atomic, Molecular $\&$
Chemical},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000235104200010},
doi = {10.1016/j.cplett.2005.11.019},
url = {https://juser.fz-juelich.de/record/57916},
}