Dr. Alessandro Senes
Assistant Professor of Biochemistry
University of Wisconsin-Madison
Madison, WI

Monday, October 7, 2013
3:00 pm (CT)
3269 Beckman Institute

Abstract

Membrane proteins comprise 20-30% of all proteins. They are responsible for many essential biological functions; yet, determining their structure with the traditional methods (X-ray crystallography, NMR) remains extremely challenging. The goal of my laboratory is to develop computational and biophysical methods as an avenue to investigate the structure/function relationship of these systems. We are interested in understanding the structural organization of the bacterial cell division complex, a large multi-protein assembly called the “divisome”. The divisome has been extensively studied in vivo using molecular genetics methods, but its precise structural organization remains unclear. Using an integration of molecular modeling, biophysical measurements, mutagenesis and crystallography we have begun to unravel the physical interactions and the structure of some of the components this important complex. We are also interested in developing general methods that will help advance the structural understanding of complexes of membrane proteins. In the second part of my talk I will present our efforts to predict computationally the structure of oligomeric complexes of transmembrane helices. We have developed a method that exploits both “canonical” and “weak” hydrogen bonds as geometric constraints to guide structure prediction. This method, called CATM, predicts known structures with high accuracy, and it is now being applied to identify interesting structural candidates at the genome wide level.