High pressure small-angle neutron scattering study of the aggregation state of beta-lactoglobulin in water and in water/ethylene-glycol solutions (Articolo in rivista)

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Label
  • High pressure small-angle neutron scattering study of the aggregation state of beta-lactoglobulin in water and in water/ethylene-glycol solutions (Articolo in rivista) (literal)
Anno
  • 2006-01-01T00:00:00+01:00 (literal)
Alternative label
  • Ortore, MG; Spinozzi, F; Carsughi, F; Mariani, P; Bonetti, M; Onori, G (2006)
    High pressure small-angle neutron scattering study of the aggregation state of beta-lactoglobulin in water and in water/ethylene-glycol solutions
    in Chemical physics letters (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Ortore, MG; Spinozzi, F; Carsughi, F; Mariani, P; Bonetti, M; Onori, G (literal)
Pagina inizio
  • 342 (literal)
Pagina fine
  • 346 (literal)
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  • 418 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Univ Politecn Marche, Dipartimento Sci Applicat Sist Complessi, I-60131 Ancona, Italy; Univ Perugia, Dipartimento Fis, CEMIN, I-06123 Perugia, Italy; INFM, CRS, SOFT, I-06123 Perugia, Italy; Forschungszentrum Julich, Inst Festkorperforsch, D-52425 Julich, Germany; CEA Saclay, Serv Phys Etat Condense, F-91191 Gif Sur Yvette, France (literal)
Titolo
  • High pressure small-angle neutron scattering study of the aggregation state of beta-lactoglobulin in water and in water/ethylene-glycol solutions (literal)
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. (literal)
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