Published in

International Union of Crystallography, Acta Crystallographica Section D: Biological Crystallography, 10(58), p. 1554-1559, 2002

DOI: 10.1107/s0907444902014397

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Thermodynamic relationships between protein-solvent and protein-protein interactions

Journal article published in 2002 by Lionel Costenaro, Christine Ebel ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

How the solvent modulates the weak inter-particle interactions in solution and affects macromolecule solubility is not yet understood. Well-established thermodynamic relationships link second virial coefficient and preferential solute binding parameter. We present the meaning of these thermodynamic parameters and the way to measure them. When a solvation shell has a composition different from the bulk solvent, a negative contribution is found in the second virial coefficient corresponding to an effective attraction between the macromolecules in solution. A quantitative evaluation using simple models of solvated particles in solution suggests that solvation could induce, at high or low concentration of a small molecule solute, attractive inter-particle interactions corresponding to favorable crystallization conditions.