Thermodynamic relationships between protein-solvent and protein-protein interactions.
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.
D001665:Binding Sites; D003461:Crystallography; D046911:Macromolecular Substances; D009997:Osmotic Pressure; D011506:Proteins / Q000737:chemistry*; D012995:Solubility; D012997:Solvents; D013816:Thermodynamics; D014867:Water
D046911:Macromolecular Substances; D011506:Proteins; D012997:Solvents; D014867:Water