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| Home > Publications database > High pressure small-angle scattering study of the aggregation state of beta-lactoglobulin in water and in water/ethylene-glycol solutions |
| Home > Publications database > High pressure small-angle scattering study of the aggregation state of beta-lactoglobulin in water and in water/ethylene-glycol solutions |
| Journal Article | PreJuSER-57916 |
; ; ; ; ;
2006
Elsevier
Amsterdam [u.a.]
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Please use a persistent id in citations: doi:10.1016/j.cplett.2005.11.019
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.
Keyword(s): J
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