Lynmarie Thompson

Condensed Biography:

Postdoctoral Fellow, Massachusetts Institute of Technology (1989–1990)
Ph.D., Yale University (1989)
B.S., California Institute of Technology (1983)

Affiliations:

President-elect, Biophysical Society
Faculty, Graduate Program in Molecular & Cellular Biology
Faculty, Models to Medicine, Institute for Applied Life Sciences

Research Interests: 

Membrane proteins perform functions critical to life processes, so a large fraction of drug targets are membrane proteins. Our lab investigates the structure and mechanism of bacterial chemotaxis receptor signaling complexes. Since chemotaxis is critical to some pathogenic bacteria, this work may open doors to for the development of novel antibiotics. And since many key biological processes occur in complexes of multiple proteins, the strategies we develop for this system will have widespread important applications.

Our research program has demonstrated that protein dynamics, disorder, and stability are important aspects of the signaling mechanism. We use and develop various tricks to assemble native-like, functional signaling complexes in the kinase-on and kinase-off signaling states, and then apply biophysical methods to compare the structure and dynamics and deduce the mechanism. Current projects in the lab use solid-state NMR, solution NMR, and hydrogen exchange mass spectrometry (HDX-MS). These studies have revealed that the receptor cytoplasmic domain has remarkably dynamic segments and partial disorder within functional complexes, and that signaling involves stabilization of multiple proteins in the complex. We are taking advantage of the dynamic properties of the receptor to focus our NMR experiments on the protein interfaces in these functional complexes, and aim to detect how these interfaces change to propagate the signal.