Effective potential between negatively charged patches on acidic proteins immersed in various electrolyte solutions.

Effective interactions between O-sized anions in various electrolyte solutions were calculated by using the integral equation theory with some simple models. The results indicated that only multivalent cations mediated a strong effective attraction between O-sized anions at a certain concentration. The effective interaction turned from repulsive to attractive as the electrolyte concentration increased, and the effective attraction decreased when more electrolyte was added. Moreover, the effective interactions between O-sized anions in the electrolyte solution did not present a long repulsive tail, although the effective attraction caused by the divalent cations appeared. By contrast, the effective attraction mediated by monovalent cations and the reentrant behavior did not appear and the effective interaction was basically repulsive. These behaviors agree with the experimental results for reentrant condensation of acidic proteins in various electrolyte solutions. The calculated results suggest that the dissociated carboxylic acidic groups on the proteins form attractive patches between proteins under certain concentration conditions.