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000057916 084__ $$2WoS$$aChemistry, Physical
000057916 084__ $$2WoS$$aPhysics, Atomic, Molecular & Chemical
000057916 1001_ $$0P:(DE-HGF)0$$aOrtore, M. G.$$b0
000057916 245__ $$aHigh pressure small-angle scattering study of the aggregation state of beta-lactoglobulin in water and in water/ethylene-glycol solutions
000057916 260__ $$aAmsterdam [u.a.]$$bElsevier$$c2006
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000057916 440_0 $$01200$$aChemical Physics Letters$$v418$$x0009-2614$$y4
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000057916 520__ $$aHigh-pressure SANS experiments have been performed on acidic dilute solutions of the dimeric protein P-lactoglobulin. To evidence the solvent effect on the protein stability during compression, two different solvents, D2O and a 50% w/w mixture of water and ethyleneglycol have been considered. Data confirm that pressure induces dissociation in both solvents, even if P-lactoglobulin shows an higher stability in 50% ethylene-glycol. An original global fitting procedure has been used to derive the thermodynamic parameters that describe the dissociation equilibrium. As a result, the role of the solvent in protein dissociation has been observed to reflect on volume and compressibility changes. (c) 2005 Elsevier B.V. All rights reserved.
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000057916 7001_ $$0P:(DE-HGF)0$$aSpinozzi, F.$$b1
000057916 7001_ $$0P:(DE-Juel1)VDB2958$$aCarsughi, F.$$b2$$uFZJ
000057916 7001_ $$0P:(DE-HGF)0$$aMariani, P.$$b3
000057916 7001_ $$0P:(DE-HGF)0$$aBonetti, M.$$b4
000057916 7001_ $$0P:(DE-HGF)0$$aOnori, G.$$b5
000057916 773__ $$0PERI:(DE-600)1466293-0$$a10.1016/j.cplett.2005.11.019$$gVol. 418$$q418$$tChemical physics letters$$v418$$x0009-2614$$y2006
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000057916 9141_ $$aNachtrag$$y2006
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