Join Yale Chemistry for a Silliman Biophysical/Physical Chemistry Seminar with Paul Robustelli, Assistant Professor of Chemistry, Dartmouth College.
Abstract: Intrinsically disordered proteins (IDPs), which represent ~40% of the human proteome, play crucial roles in a variety of biological pathways and biomolecular assemblies and have been implicated in many human diseases. IDPs do not fold into a well-defined three-dimensional structure under physiological conditions. Instead, they populate a dynamic conformational ensemble of rapidly interconverting structures. As a result, IDPs are extremely difficult to experimentally characterize and are largely considered “undruggable” by conventional structure-based drug design methods. Our laboratory utilizes a combination of computational and biophysical methods to characterize the molecular recognition mechanisms of intrinsically disordered proteins in atomic detail. Here I will discuss recent progress in our efforts to characterize the interactions of IDPs with small molecule drugs, understand molecular mechanisms that drive the formation of biomolecular condensate, and understand how small molecule drugs modulate biomolecular condensate stability.
For more information about the Robustelli group, please click here: Robustelli Group
Faculty Host: Patrick Loria
This seminar is generously sponsored by the Mrs. Hepsa Ely Silliman Memorial Fund
View this seminar online at this link: Panopto Link