Three frontiers in the thermodynamics of protein solutions*
John Prausnitz and Loddie Foose
Chemical Engineering Department, University of California, Berkeley; and Chemical Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA
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.
Keywords: proteins; crystallization; phase diagrams; calorimetry; HIV-protease inhibitors.
*Paper based on a presentation at the 19th International Conference on Chemical Thermodynamics (ICCT-19), 30 July to 4 August 2006, Boulder, CO, USA. Other presentations are published in this issue, pp. 1345-1462.