TY  - JOUR
AU  - Ortore, M. G.
AU  - Spinozzi, F.
AU  - Carsughi, F.
AU  - Mariani, P.
AU  - Bonetti, M.
AU  - Onori, G.
TI  - High pressure small-angle scattering study of the aggregation state of beta-lactoglobulin in water and in water/ethylene-glycol solutions
JO  - Chemical physics letters
VL  - 418
SN  - 0009-2614
CY  - Amsterdam [u.a.]
PB  - Elsevier
M1  - PreJuSER-57916
PY  - 2006
N1  - Record converted from VDB: 12.11.2012
AB  - 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.
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000235104200010
DO  - DOI:10.1016/j.cplett.2005.11.019
UR  - https://juser.fz-juelich.de/record/57916
ER  -