%0 Journal Article
%A Ortore, M. G.
%A Spinozzi, F.
%A Carsughi, F.
%A Mariani, P.
%A Bonetti, M.
%A Onori, G.
%T High pressure small-angle scattering study of the aggregation state of beta-lactoglobulin in water and in water/ethylene-glycol solutions
%J Chemical physics letters
%V 418
%@ 0009-2614
%C Amsterdam [u.a.]
%I Elsevier
%M PreJuSER-57916
%D 2006
%Z Record converted from VDB: 12.11.2012
%X 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.
%K J (WoSType)
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000235104200010
%R 10.1016/j.cplett.2005.11.019
%U https://juser.fz-juelich.de/record/57916