Katherine Henzler-Wildman, Ph.D.
Office: 2808 North Building
The Henzler-Wildman lab is interested in the functional importance of membrane protein dynamics. Membrane proteins are active molecules that perform critical tasks relaying signals and molecules across the cell membrane and across membrane barriers within the cell. To fully understand the function of these proteins, not only the structure, but the timescale, amplitude, and directionality of structural changes must be determined.
We are currently studying the small multidrug resistance transporter EmrE. The cartoon presents a model of the conformational changes believed to occur during the EmrE transport cycle. Our research combines atomic resolution structural data and quantitative dynamics information obtained from NMR spectroscopy with traditional activity assays to build a molecular model of the transport process and study the mechanism of transporter-driven multidrug resistance.
Most Recent Publications
- Dutta, S., Morrison, E.A. and Henzler-Wildman, K.A. Blocking dynamics of the SMR transporter EmrE impairs efflux activity. Biophys J (E-pub ahead of print.) (2014) [Abstract]
- Dutta, S., Morrison, E.A. and Henzler-Wildman, K.A. EmrE dimerization depends on membrane environment. Biochim Biophys Acta 1838:1817-1822 (2014) [Abstract]
- Morrison, E.A. and Henzler-Wildman, K.A. Transported substrate determines exchange rate in the multidrug resistance transporter EmrE. J Biol Chem 289:6825-6836 (2014) [Abstract]
- Batchelor, J.D., Malpede, B.M., Omattage, N.S., Dekoster, G.T., Henzler-Wildman, K.A. and Tolia, N.H. Red blood cell invasion by Plasmodium vivax: Structural basis for DBP engagement of DARC. PloS Pathog. 10:e1003869 (2014) [Abstract]
- Morrison, E.A. and Henzler-Wildman, K.A. Reconstitution of integral membrane proteins into isotropic bicelles with improved sample stability and expanded lipid composition profile. Biochim Biophys Acta 1818:814-820 (2012). [Abstract]
- Henzler-Wildman, K.A. Analyzing conformational changes in the transport cycle of EmrE. Curr Opin Struct Biol 22:38-43 (2012). [Abstract]
- Morrison, E.A., DeKoster, G.T., Dutta, S., Vafabgakhsh, R., Clarkson, W., Bahl, A., Kern, D., Ha, T. and Henzler-Wildman, K.A. Antiparallel EmrE Exports Drugs by Exchanging Between Asymmetric Structures. Nature 481:45-50 (2011). [Abstract]
- Ramamoorthy, A., Lee, D-K., Santos, J.S. and Henzler-Wildman, K.A. Nitrogen-14 Solid-state NMR spectroscopy of aligned phospholipid bilayers to probe peptide-lipid interaction and oligomerization of membrane associated peptides. J. Am. Chem. Soc. 130:11023–11029 (2008). [Abstract]
- Porcelli, F., Verardi, R., Shi, L., Henzler-Wildman, K.A., Ramamoorthy, A., and Veglia, G. NMR Structure of the cathelicidin-derived human antimicrobial peptide LL-37 in dodecylphosphocholine micelles. Biochemistry, 47:5565–5572 (2008). [Abstract]
- Henzler-Wildman K.A. and Kern D. Dynamic personalities of proteins. Nature 450:964-972 (2007). [Abstract]
- Henzler-Wildman K.A., Lei M., Thai V., Kerns S.J., Karplus M., and Kern D. A hierarchy of timescales in protein dynamics is linked to enzyme catalysis. Nature 450:913-916 (2007). [Abstract]
- Henzler-Wildman K.A., Thai V., Lei M., Ott M., Wolf-Watz M., Fenn T., Pozharski E., Wilson M.A., Petsko G.A., Karplus M., Hübner C.G., and Kern, D. Intrinsic motions along an enzymatic reaction trajectory. Nature 450:838-844 (2007). [Abstract]
- Moon, J.Y., Henzler-Wildman, K.A. and Ramamoorthy, A. Expression and purification of a recombinant LL-37 from Escherichia coli. Biochim Biophys Acta 1758:1351-1358 (2006). [Abstract]