Faculty

Katie Henzler-Wildman’s laboratory studies the relationship between structure, dynamics and function in ion channels and transporters. Her group uses cutting-edge NMR spectroscopy methods to measure the relative populations of different protein structural states and the rate of transition between them. Combining this data with traditional biophysical and biochemical functional assays provides insight into the detailed molecular mechanism of these integral membrane proteins. The Henzler-Wildman lab studies small multidrug resistance transporters, proton-coupled transporters that contribute to antibiotic resistance in bacteria by pumping a broad range of toxic substrates out of the bacterial cytoplasm. The two goals of this project are to understand the mechanism of secondary active transport and how these tiny transporters recognize and actively efflux such diverse substrates. A second project investigates fundamental ion channel function: How do channels achieve ion selectivity? How do channels sense diverse environmental stimuli and couple that to drive opening or closing of the pore? In all of these projects, NMR data on protein conformational states and structural transitions are analyzed in conjunction with quantitative biophysical and functional assays to develop kinetic models for how these transporters and channels work on the molecular level.