About the Seminar:

Proteins operate within an aqueous environment that influences their folding, stability, and activity. Membrane proteins have the added complication of being embedded in lipid bilayers that play an equally critical, yet significantly less understood, role. Much like solvent conditions modulate enzyme kinetics and protein interactions in solution, the lipid composition of the membrane performs regulatory functions for membrane proteins, affecting their organization, conformational dynamics, and catalytic output. To investigate these membrane-dependent phenomena, we employ time-resolved fluorescence spectroscopy techniques like pulsed interleaved excitation fluorescence cross-correlation spectroscopy (PIE-FCCS) in model membranes and live cells. We couple these spectroscopic probes with liposome-based activity assays in vitro. These complementary approaches allow us to quantitatively assess how specific lipid species influence the assembly and function of receptor tyrosine kinases (RTKs). By drawing parallels to the well-established influence of solvent on soluble proteins, our work centers the membrane environment as a dynamic and tunable component of cell signaling.

About the speaker:

Adam W. Smith was born in Texas and grew up in Utah. He was an undergraduate at the University of Utah and then earned a PhD at MIT in the lab of Andrei Tokmakoff studying peptide and protein folding with 2D IR spectroscopy. From 2008-2011 he was a postdoctoral researcher with Jay T. Groves at UC Berkeley, where he studied membrane protein structure and function with advanced fluorescence imaging and spectroscopy. In 2012, Adam was a visiting scientist at the National University of Singapore and Lawrence Berkeley National Laboratory. He joined the faculty at the University of Akron from 2012-2022 and then moved to Texas Tech University where he is currently an Associate Professor of Chemistry.