A.B., Chemistry, Princeton University
Ph.D., Chemistry, Yale University
Postdoctoral Fellow, Chemistry, University of Pennsylvania
I teach at all levels of the curriculum including physical chemistry, integrated experimental chemistry, introductory chemistry, and advanced topics seminars in biophysical chemistry.
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 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.
Recent publications *Undergraduate co-author
Kim G.*, Raymond, H.E.*, Herneisen, A.L.*, Wong-Rolle, A.* and Howard, K.P. (2019) The distal cytoplasmic tail of the influenza A M2 protein dynamically extends from the membrane. Biochimica Biophysica Acta – Biomembranes, 1861, 1421-1427. DOI: 10.1016/j.bbamem.2019.05.021
Crouch, C., Bost, M.*, Kim, T.*, Green, B.*, Arbuckle, D.S.*, Grossman, C. and Howard, K.P. (2018) Optimization of Detergent-Mediated Reconstitution of Influenza A M2 Protein into Proteoliposomes. Membranes, 8, 103. DOI:10.3390/membranes8040103
Herneisen, A.L.*, Sahu, I.D., McCarrick, R.M., Feix, J.B., Lorigan, G.A. and Howard, K. P. (2017) A Budding-Defective M2 Mutant Exhibits Reduced Membrane Interaction, Insensitivity to Cholesterol, and Perturbed Interdomain Coupling. Biochemistry, 56, 5955. DOI: 10.1021/acs.biochem.7b00924
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. 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, 24, 426. (selected as a "Highlight" of the issue by the journal editors) DOI: 10.1002/pro.2631
To learn more about my research please visit my research group webpage.