Lynmarie K. Thompson
Research areas include structure of ligands bound to membrane proteins by solid-state NMR, site-directed local structure of functional states of membrane-bound receptors and complexes, hydrogen exchange measurements of protein stability and dynamics in functional membrane-bound protein complexes, bacterial signaling systems, and microbial ABC transporters involved in ethanol production.
Current Research
My research focus is on understanding how membrane proteins mediate key life processes such as sensing, signaling, and transport. Our biophysical and biochemical studies of sensing and signaling by bacterial chemotaxis receptors have potential applications in the development of antibiotics, as these proteins function in two-component signaling systems that are critical to bacteria but not found in mammals. Another project investigating carbohydrate transport by bacterial ABC transporters is relevant to human digestion and to biofuel production.
My laboratory develops and implements novel approaches to assemble functional states of membrane protein complexes and novel approaches to measure local structure and dynamics to gain insights into the molecular mechanisms. Our achievements regarding the mechanism of bacterial chemotaxis receptors include:
- The first site-directed distance measurement of a tiny (≈2 Å) mechanistically important conformational change in the intact membrane-bound receptor
- Demonstration that kinase control by this receptor does not involve ligand-induced receptor dissociation, key evidence for settling a long-standing controversy over the role of clustering in the signal
- Demonstration of the dynamic nature of the receptor cytoplasmic domain and significant reduction of these dynamics upon assembly of functional complexes
- Measurements that complement crystal structures by revealing a difference in the protein-protein contacts in functional complexes
For our current research we assemble native-like nanoarrays (200 nm dimensions) of chemotaxis receptors with their partner proteins in defined signaling states. We use activity measurements, NMR measurements, and hydrogen exchange mass spectrometry to test proposed changes in structure and dynamics between these signaling states and to develop models for the mechanism of signal propagation.
Learn more at people.chem.umass.edu/thompson
Academic Background:
- BS 1983, California Institute of Technology
- PhD 1989, Yale University
- Jane Coffin Childs Postdoctoral Fellow 1989-1990, Massachusetts Institute of Technology
