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Journal of Chemical Physics / Volume 135 / Issue 24 / ARTICLES / Biological Molecules, Biopolymers, and Biological Systems

J. Chem. Phys. 135, 245103 (2011); http://dx.doi.org/10.1063/1.3670419 (9 pages)

Preferential solvation of lysozyme in water/ethanol mixtures

Maria Grazia Ortore1, Paolo Mariani1, Flavio Carsughi2,3, Stefania Cinelli4, Giuseppe Onori4, José Teixeira5, and Francesco Spinozzi1

1Department of Life and Environment Sciences, Marche Polytechnic University and CNISM, I-60131 Ancona, Italy
2Department of Agricultural Food and Environmental Sciences, Marche Polytechnic University and CNISM, I-60131 Ancona, Italy
3Jülich Center for Neutron Scattering, Forschungszentrum Jülich, D-85747 Garching, Germany
4Department of Physics, University of Perugia and CEMIN, I-06123 Perugia, Italy
5Laboratoire Léon-Brillouin, F-91191 Gif-sur-Yvette, France

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(Received 30 June 2011; accepted 29 November 2011; published online 23 December 2011)

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 ethanol molar fraction ≈0.06, corresponding to the triggering of the hydrophobic clustering of alcohol molecules detected in water/ethanol binary mixtures.

© 2011 American Institute of Physics

Article Outline

  1. INTRODUCTION
  2. MATERIALS AND METHODS
    1. Sample preparation
    2. SANS experiments
    3. DSC data
  3. THERMODYNAMIC MODEL AND DATA ANALYSIS
    1. Solvent exchange thermodynamic model
    2. SANS data analysis
    3. DSC data analysis
    4. Global fit analysis
  4. RESULTS AND DISCUSSION

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KEYWORDS and PACS

Keywords

biochemistry, bonds (chemical), differential scanning calorimetry, liquid mixtures, macromolecules, molecular biophysics, neutron diffraction, proteins, reaction kinetics, segregation, solvation, water

PACS

ARTICLE DATA

Digital Object Identifier
http://dx.doi.org/10.1063/1.3670419

PUBLICATION DATA

ISSN

0021-9606 (print)  
1089-7690 (online)

Publisher

$abstract.society.value is a Member of CrossRef American Institute of Physics

For access to fully linked references, you need to log in.
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    F. Spinozzi, M. G. Ortore, R. Sinibaldi, P. Mariani, A. Esposito, S. Cinelli, and G. Onori, J. Chem. Phys. 129, 35101 (2008)JCPSA6000129000003035101000001.

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