Interactions at surfaces define the reactivity of proteins, whether this be plastic wall in your milk jug, the polymer contact in your eye, or the permeable membrane in a chromatographic column. Our research attempts to characterize the dynamics of these interactions using single-molecule, super-resolution fluorescence microscopy. In doing so, we hope to identify the mechanisms that foul membranes, inhibit protein motion, and detract from successful separations. We can achieve this by considering the protein conformational changes, kinetics of protein interactions, and the motion of proteins exploring the surface.
Chatterjee, S., A., Carina, Nurik, C.E., Carrejo, N.C., Dutta, C., Jayaraman, V., Landes, C.F., "Phosphorylation Induces Conformational Rigidity at the C-Terminal Domain of AMPA Receptors" J. Phys. Chem. B 2019
Dolino, D.M., Chatterjee, S., MacLean, D.M., Flatebo, C., Bishop, L.D.C., Shaikh, S.A., Landes, C.F., Jayaraman, V., "The structure–energy landscape of NMDA receptor gating" Nat. Chem. Bio., 2017, 13, pp. 1232-1238
Poongavanam, M. -V.; Kisley, L.; Kourentzi, K.; Willson, R.C.; Landes, C. F., "Ensemble and single-molecule biophysical characterization of D17.4 DNA aptamer–IgE interactions" BBA Proteins Proteom. 2016, 1864, 154-164.
Cooper, D.; Dolino, D.; Jaurich, H.; Shuang, B.; Ramaswamy, S.; Nurik, C.E.; Chen, J.; Jayaraman, V.; Landes, C. F., "Conformational Transitions in the Glycine-Bound GluN1 NMDA Receptor LBD via Single-Molecule FRET" Biophys.J, 2015, 109, 66 - 75