Solvation and solubility of globular proteins

Abstract

The solvation Gibbs energy of proteins is expressed in terms of its various ingredients (refs. 1,2). Estimation of the magnitude of these ingredients can lead to an estimate of the overall solvation Gibbs energy of the protein. As expected, the hydrophilic groups exposed to the solvent are mainly responsible for the solubility of the protein. However, we also found, unexpectedly, that correlation between hydrophilic groups on the surface of the protein can have a decisive contribution to the solvation Gibbs energy, and hence to the solubility of the protein.