Understanding and manipulating protein-protein interactions in membranes

POLY 33

William F DeGrado, wdegrado@mail.med.upenn.edu, Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, 1009 Stellar Chance laboratories, 36th and Hamilton Walk, Philadelphia, PA 19104-6059
This talk will focus on the assembly and function of transmembrane helical proteins. Proteins with single transmembrane (TM) helices represent a functionally diverse class of structures, and important members of the helical class of membrane proteins. Not long ago single-span TM helices were considered to be mere anchors for more “interesting” water-soluble protein domains. More recently, single-pass TM helices have been shown to be essential for directing the assembly of protein complexes and mediating signal transduction – playing roles analogous to leucine zippers, helix-loop-helix motifs, coiled-coils, and other small modules in water-soluble proteins. Our goals are: 1) to use natural self-assembling TM systems to learn the rules of membrane protein folding, and 2) to design synthetic peptides that target TM domains in much the same way that antibodies target water-soluble regions of natural proteins.
 

Herman Mark Scholar Award Symposium
8:30 AM-11:55 AM, Sunday, August 19, 2007 Westin Boston Waterfront -- Grand Ballroom C, Oral

Division of Polymer Chemistry

The 234th ACS National Meeting, Boston, MA, August 19-23, 2007