UMBC logo
UMBC Department of Physics
News & Events

About

This page contains a single entry from the blog posted on September 8, 2010 3:30 AM.

The previous post in this blog was Seminar: Wednesday, September 1, 2010 at 3:30 p.m..

The next post in this blog is Seminar: Wednesday, September 15, 2010 at 3:30 p.m. Coffee at 3:15 pm.

Many more can be found on the main index page or by looking through the archives.

Powered by
Movable Type 3.34

« Seminar: Wednesday, September 1, 2010 at 3:30 p.m. | Main | Seminar: Wednesday, September 15, 2010 at 3:30 p.m. Coffee at 3:15 pm »

Seminar: Wednesday, September 8, 2010 at 3:30 p.m. Coffee 3:15 p.m.

Using molecular simulations to understand allosteric inhibition of the Hepatitis C viral polymerase
Dr. Ian Thorpe
UMBC/Chemistry Department
The general term "allostery" is often used to refer to processes which allow an event at one location in a macromolecule (such as a protein) to alter the properties of another location in that macromolecule. Allostery is important because it allows macromolecules such as proteins to sense and respond to their environment, providing a way to regulate their functional characteristics. Thus, understanding the physical principles which underlie allostery can be of significant utility in understanding how proteins and other macromolecules function. Allostery can occur because distant regions of a macromolecule are structurally connected, potentially allowing information to be communicated over long distances within the molecule. Allosteric inhibitors of the RNA-dependent RNA polymerase (RdRp) found in Hepatitis C Virus (HCV) have been identified which bind to the enzyme distant from the site of catalysis. The manner in which these ligands inhibit the enzyme is not well understood. I will describe efforts in my research group to understand the link between ligand binding and allosteric inhibition in RdRp by using molecular simulation methods to describe the structure and dynamics of this enzyme. The knowledge gained as a result of this study can improve our understanding of allosteric regulation of enzyme function and the manner in which the process may be modulated by small molecules. In addition, these studies may foster the development of new treatments for HCV infections.
UMBC's Department of Physics   |   410-455-2513 or 1-877-707-1969 (toll free)   |   physics@umbc.edu  |  Site Info