Home > Publications database > Preferential solvation of lysozyme in water/ethanol mixtures |
Journal Article | FZJ-2015-03387 |
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2011
American Institute of Physics
Melville, NY
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Please use a persistent id in citations: http://hdl.handle.net/2128/19003 doi:10.1063/1.3670419
Abstract: 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.
Keyword(s): Health and Life (1st) ; Biology (2nd) ; Soft Condensed Matter (2nd)
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