TY  - JOUR
AU  - Ortore, Maria Grazia
AU  - Mariani, Paolo
AU  - Carsughi, Flavio
AU  - Cinelli, Stefania
AU  - Onori, Giuseppe
AU  - Teixeira, José
AU  - Spinozzi, Francesco
TI  - Preferential solvation of lysozyme in water/ethanol mixtures
JO  - The journal of chemical physics
VL  - 135
IS  - 24
SN  - 0021-9606
CY  - Melville, NY
PB  - American Institute of Physics
M1  - FZJ-2015-03387
SP  - 245103
PY  - 2011
AB  - We provide a quantitative description of the solvation properties of lysozyme in water/ethanol mixtures, which has been obtained by a simultaneous analysis of small-angle neutron scattering and differential scanning calorimetry experiments. All data sets were analyzed by an original method, which integrates the exchange equilibrium model between water and ethanol molecules at the protein surface and activity coefficients data of water/ethanol binary mixtures. As a result, the preferential binding of ethanol molecules at the protein surface was obtained for both native and thermal unfolded protein states. Excess solvation numbers reveal a critical point at ethanolmolar fraction ≈0.06, corresponding to the triggering of the hydrophobic clustering of alcohol molecules detected in water/ethanol binary mixtures.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000298640500054
DO  - DOI:10.1063/1.3670419
UR  - https://juser.fz-juelich.de/record/201077
ER  -