Journal Article FZJ-2015-03387

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Preferential solvation of lysozyme in water/ethanol mixtures

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2011
American Institute of Physics Melville, NY

The journal of chemical physics 135(24), 245103 () [10.1063/1.3670419]

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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)

Classification:

Contributing Institute(s):
  1. JCNS-FRM-II (JCNS (München) ; Jülich Centre for Neutron Science JCNS (München) ; JCNS-FRM-II)
  2. Neutronenstreuung (Neutronenstreuung ; JCNS-1)
  3. Streumethoden (JCNS-2)
Research Program(s):
  1. 54G - JCNS (POF2-54G24) (POF2-54G24)
Experiment(s):
  1. Measurement at external facility

Database coverage:
Medline ; OpenAccess ; Current Contents - Physical, Chemical and Earth Sciences ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection
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Institute Collections > JCNS > JCNS-1
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 Record created 2015-06-03, last modified 2024-06-19