Prediction of Hofmeister ion effects on biopolymer processes

PHYS 328

Laurel M. Pegram, lmpegram@wisc.edu, Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706 and M. Thomas Record Jr., record@biochem.wisc.edu, Departments of Chemistry and Biochemistry, University of Wisconsin-Madison, 433 Babcock Drive, Madison, WI 53706.
The Hofmeister series is a qualitative ranking of salt anions and cations originally based on their effectiveness (typically at molar concentrations) as protein precipitants and subsequently extended to other processes in which water-accessible protein surface area (ASA) changes significantly (folding, assembly). Application of a novel two-domain salt ion partitioning model (SPM) to thermodynamic data on the effects of Hofmeister salts on model processes (surface tension, model compound solubility) provides a molecular thermodynamic description of ions at uncharged interfaces. Resulting local-bulk partition coefficients along with a coarse-grained description of functional groups that make up a molecular surface have provided successful predictions of noncoulombic salt effects on micelle formation, protein folding, and DNA melting.
 

PHYS Poster Session - Water Mediated Interactions
7:30 PM-10:00 PM, Wednesday, August 20, 2008 Pennsylvania Convention Center -- Hall C, Poster

Division of Physical Chemistry

The 236th ACS National Meeting, Philadelphia, PA, August 17-21, 2008