Rate My Professor Lynmarie Thompson

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.