Randy Stockbridge graduated from Princeton University with an A.B. in Molecular Biology in 2005.  She went on to study with Richard Wolfenden at the University of North Carolina at Chapel Hill, and received a Ph.D. in Biochemistry and Biophysics in 2010.   She did her postdoctoral work with Chris Miller at Brandeis University.  Her lab tackles mechanisms and structures of membrane transport proteins using electrophysiology, biochemistry and biophysics, and x-ray crystallography. 


Membrane transporter proteins – channels and energy-coupled pumps – are the molecular gatekeepers of the cell.  For microbes afloat in a hostile environment, these proteins import vital nutrients and export dangerous toxins.  My lab is currently focused on understanding the export of F- anion, an inhibitor of glycolysis and protein synthesis that bacteria, archaea, unicellular eukaryotes, and plants have confronted in their environmental milieu over evolutionary time.  Specific F- export isn’t an easy task since the ion’s radius only differs by half an Angstrom from that of the world’s most abundant aqueous ion, Cl-.   Two different membrane protein families have evolved to accomplish it: the Fluc family of fluoride channels, and the CLCFfamily of F-/H+ antiporters. My laboratory is investigating the molecular mechanism of both classes of protein, using a breadth of biochemical and biophysical techniques, including electrophysiology, membrane protein biochemistry, x-ray crystallography, and macromolecular NMR.