作者: Maria Grazia Ortore , Paolo Mariani , Flavio Carsughi , Stefania Cinelli , Giuseppe Onori
DOI: 10.1063/1.3670419
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摘要: We provide a quantitative description of the solvation properties lysozyme in water/ethanol mixtures, which has been obtained by simultaneous analysis small-angle neutron scattering and differential scanning calorimetry experiments. All data sets were analyzed an original method, integrates exchange equilibrium model between water ethanol molecules at protein surface activity coefficients binary mixtures. As result, preferential binding was for both native thermal unfolded states. Excess numbers reveal critical point molar fraction ≈0.06, corresponding to triggering hydrophobic clustering alcohol detected