Protein-protein interactions in concentrated electrolyte solutions.

摘要: Protein-protein interactions were measured for ovalbumin and lysozyme in aqueous salt solutions. are correlated with a proposed potential of mean force equal to the free energy desolvate protein surface that is made inaccessible solvent due protein-protein interaction. This calculated from determined protein-salt preferential-interaction parameter measurements. In classical salting-out behavior, preferential interaction unfavorable. Because addition raises according surface-tension increment salt, attraction increases, leading reduction solubility. When chemistry proteins altered by binding specific ion, salting-in observed when between (kosmotrope) ion-protein complexes more repulsive than those uncomplexed proteins. However, (chaotrope) attractive