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000201077 1001_ $$0P:(DE-HGF)0$$aOrtore, Maria Grazia$$b0
000201077 245__ $$aPreferential solvation of lysozyme in water/ethanol mixtures
000201077 260__ $$aMelville, NY$$bAmerican Institute of Physics$$c2011
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000201077 520__ $$aWe 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.
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000201077 7001_ $$0P:(DE-HGF)0$$aMariani, Paolo$$b1
000201077 7001_ $$0P:(DE-Juel1)130587$$aCarsughi, Flavio$$b2
000201077 7001_ $$0P:(DE-HGF)0$$aCinelli, Stefania$$b3
000201077 7001_ $$0P:(DE-HGF)0$$aOnori, Giuseppe$$b4
000201077 7001_ $$0P:(DE-HGF)0$$aTeixeira, José$$b5
000201077 7001_ $$0P:(DE-HGF)0$$aSpinozzi, Francesco$$b6$$eCorresponding Author
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