Three frontiers in the thermodynamics of protein solutions

Abstract

Three examples illustrate the versatility and usefulness of biothermodynamics. The first example concerns calculation of a phase diagram for aqueous lysozyme with a new potential of mean force that takes the Hofmeister effect into account; such calculations may be useful for design of a separation process where addition of a salt to an aqueous protein mixture precipitates a target protein. The second example concerns thermodynamic studies to elucidate the effect of an organic cosolvent on the mechanism of crystallizing aqueous insulin. The final example concerns a thermodynamic contribution to mitigating the AIDS epidemic; it indicates how isothermal-titration-calorimetry studies are helpful for choosing an optimum inhibitor that is effective not only for the wild-type HIV protease but also for at least some of its mutants.