Rate My Professor Lynmarie Thompson

Lynmarie Thompson is a Professor of Chemistry in the Department of Chemistry at the University of Massachusetts Amherst. She serves as Director of the Chemistry-Biology Interface Predoctoral Training Program, and as faculty in the Graduate Program in Molecular and Cellular Biology and Models to Medicine at the Institute for Applied Life Sciences. Thompson earned her B.S. from the California Institute of Technology in 1983 and her Ph.D. from Yale University in 1989 under Gary Brudvig, investigating photosystem II. She completed a postdoctoral fellowship from 1989 to 1990 at the Massachusetts Institute of Technology in Robert Griffin's laboratory, applying solid-state NMR to bacteriorhodopsin photocycle intermediates.

Her research specializes in biophysical studies of membrane protein structure, dynamics, and mechanisms, focusing on bacterial chemotaxis receptor signaling complexes and ABC transporters. The Thompson laboratory assembles native-like functional complexes in kinase-active and kinase-inactive states, utilizing solid-state NMR, solution NMR, and hydrogen-deuterium exchange mass spectrometry to reveal conformational changes, protein disorder, and stability alterations during signaling. Notable findings include a ligand-induced piston mechanism in the serine chemoreceptor periplasmic domain, dynamic segments in cytoplasmic domains that stabilize upon complex formation, and kinase control via stabilization of the CheA catalytic domain. These insights inform signal transduction across membranes and hold potential for antibiotic strategies against pathogenic bacteria. Thompson's contributions are reflected in key publications, including "Cytochrome b-559 may function to protect photosystem II from photoinhibition" (Biochemistry, 1988), "Structural studies of spider silk proteins in the fiber" (Journal of Molecular Recognition, 1997), "Rotational resonance NMR study of the active site structure in bacteriorhodopsin" (Biochemistry, 1992), and "Bacterial chemoreceptor signaling complexes control kinase activity by stabilizing the catalytic domain of CheA" (Biochemistry, 2023). She was elected President of the Biophysical Society, assuming the role in February 2025 to advance biophysics research and community.