Professor Jerome Baudry of the University of Alabama-Hunstville will give a seminar titled "Protein dynamics and conformational selection of proteins' ligands" from 3:05-3:55 p.m. today, Nov. 1. Everyone is welcome to attend the seminar individually via Zoom or to come to CHEM 144 where the seminar can be viewed in person with other attendees. The talk is free and open to the public.

Baudry is the Mrs. Pei-Ling Chan Professor of Biological Sciences, University of Alabama, Huntsville; Department of Biological Sciences. He obtained his Ph.D. in Molecular Biophysics with the highest Honors from the University of Paris, UPMC/Sorbonne Universities, France. He subsequently joined the group of Klaus Schulten at the University of Illinois at Urbana-Champaign as a post-doc. After his post-doctoral work, Baudry worked in the pharmaceutical industry as a Research Scientist, and then accepted a Senior Research Scientist position back in Illinois on a non-tenure track research faculty position.

Baudry joined the University of Tennessee, Knoxville and the UT/ORNL Center for Molecular Biophysics as a tenure track Assistant Professor in 2008. In 2014, he was promoted to Associate Professor with tenure. In August 2017, he joined UAH as the Mrs. Pei-Ling Chan Professor. At UAH, Baudry's group develops and applies methods and protocols for computational drug discovery, both on small-molecules and biologicals, within academic, national laboratories and industrial collaborations.

His group is interested in using computers to identify small molecules that can bind on the surface or interior of proteins. This is a central question in chemical biology, and particularly important in modern drug discovery. The main technique is called "docking", where the binding free energies of different small molecules in proteins receptors models are estimated at different speed/accuracy levels. This is usually done on a single structure of the protein receptor. However, in the Baudry laboratory, they are looking at how the internal dynamics of protein receptors change the number, location and shape of potential binding sites for small molecules.

Simulating the molecular dynamics of the proteins shows that a subset of the protein conformations is much more likely to bind small molecules than most other protein conformations. For this reason, performing docking on a series of protein conformations, or "ensemble docking", is quickly becoming a preferred approach in computational chemical biology and drug discovery. Baudry will illustrate the power of ensemble docking, with several examples of "real world" drug discovery form his lab, and will discuss some of the challenges that are associated with this approach.

To attend the seminar virtually, please visit the Zoom link.
Meeting ID: 862 5015 5151
Passcode: Fall@2021