High-pressure SANS experiments have been performed on acidic dilute solutions of the dimeric protein b-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 ethylene- glycol have been considered. Data confirm that pressure induces dissociation in both solvents, even if b-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.
High pressure small-angle neutron scattering study of the aggregation state of beta-lactoglobulin in water and in water/ethylene-glycol solutions / Ortore, Maria Grazia; Spinozzi, Francesco; Carsughi, Flavio; Mariani, Paolo; Marco, Bonetti; Giuseppe, Onori. - In: CHEMICAL PHYSICS LETTERS. - ISSN 0009-2614. - STAMPA. - 418:(2006), pp. 342-346. [10.1016/j.cplett.2005.11.019]
High pressure small-angle neutron scattering study of the aggregation state of beta-lactoglobulin in water and in water/ethylene-glycol solutions
ORTORE, Maria Grazia;SPINOZZI, Francesco;CARSUGHI, Flavio;MARIANI, Paolo;
2006-01-01
Abstract
High-pressure SANS experiments have been performed on acidic dilute solutions of the dimeric protein b-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 ethylene- glycol have been considered. Data confirm that pressure induces dissociation in both solvents, even if b-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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
