Kathleen Howard (on leave 2016-2017)
A.B., Chemistry, Princeton University
Ph.D., Chemistry, Yale University
Postdoctoral Fellow, Department of Chemistry, University of Pennsylvania
I teach quantum mechanics and spectroscopy, integrated experimental chemistry, general chemistry, and an advanced seminar in biophysical chemistry. I also mentor students engaged in research for credit.
The research in my lab focuses on the use of magnetic resonance spectroscopy to investigate the structural and dynamic properties of membrane-bound molecules. Membrane proteins (which comprise 25-30% of all proteins) carry out many important biological functions including transport of material across membrane and acting as receptors. We are interested in developing and applying electron paramagnetic resonance (EPR) and nuclear magnetic resonance (NMR) spectroscopic techniques to the study of membrane associated proteins.
Kim, S.*, Upshur, M.A.*, Saotome, K.*, Sahu, I.D., McCarrick, R.M., Feix, J.B., Lorigan, G.A. and Howard, K. P. (2015) Cholesterol dependent conformational exchange of the C-terminal domain of the influenza A M2 protein. Biochemistry, 2015, 54 (49), 7157–7167. DOI: 10.1021/acs.biochem.5b01065.
Huang, S.*, Green, B.,* Thompson, M.*, Chen, R.*, Thomaston, J., DeGrado, W. and Howard, K.P. (2015) C-terminal juxtamembrane region of the full-length M2 protein forms a membrane surface associated amphipathic helix. Protein Science. (selected as a "Highlight" of the issue by the journal editors) DOI: 10.1002/pro.2631.
Saotome, K.*, Duong-Ly, K.* and Howard, K.P. (2015) Influenza A M2 protein conformation depends on choice of model membrane. Bioploymers. 104(4), 405-411. DOI: 10.1002/bip.22617.
Thomaston, J.L.*, Nguyen, P.A.*, Brown, E. C.*, Upshur, M.A.*, Wang, J. DeGrado, W.F. and Howard, K. P. (2013) "Detection of drug-induced conformational change of a transmembrane protein in lipid bilayers using site-directed spin labeling" Protein Science, 22 (1): 65-73. (selected as a "Highlight" of the issue by the journal editors) DOI: 10.1002/pro.2186.
To learn more about my research please visit my research group webpage.