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Room 304, Chemistry Building

Exposing the Moving Parts of Proteins using NMR Spectroscopy


Professor Jeff Peng
University of Notre Dame

Hosted by: Professor John Bushweller

A common metaphor for protein molecules is that they are Nature’s nanomachines.  Importantly, many of these natural nanomachines have internal moving parts – they are dynamic. Hence, whether and how intrinsic protein mobility contributes to protein mechanism are persistent questions in biology.  Nuclear magnetic resonance (NMR) spectroscopy can characterize molecular dynamics site-specifically, and over a broad time scale.  Accordingly, this presentation will focus on our use of NMR to understand the interplay between protein dynamics and mechanism in modular (multi-domain) proteins. In particular, the presentation will describe our flexibility-function studies of a small two-domain protein, human Pin1. Pin1 is a peptidyl-prolyl isomerase that is essential for mitosis. It consists of a catalytic PPIase domain and WW domain, connected by a flexible linker. Our Pin1 results suggest that protein dynamics assists both ligand recognition, as well as long-range intraprotein communication between distal functional sites.