Mei Hong

Mei Hong

Professor of Chemistry

617-253-5521

NW14-3212

Biography

Education

Ph.D. in Chemistry, University of California Berkeley (1996)
B. A. in Chemistry, summa cum laude, Mount Holyoke College (1992)

Research

We develop and apply solid-state NMR techniques to elucidate the structure and dynamics of membrane proteins and other biological macromolecules. We are especially interested in ion channels and curvature-inducing membrane proteins such as antimicrobial peptides and viral fusion proteins. Our research has elucidated the drug binding location and inhibition mechanism and proton-conduction mechanism of the influenza M2 proton channel, the conformational and dynamical changes of a channel-forming colicin that mediate its spontaneous insertion into the lipid membrane, and the membrane-bound oligomeric structure of β-hairpin antimicrobial peptides and the mechanism with which these cationic molecules insert into lipid membranes against the free energy barrier. We also investigate other macromolecules such as elastin and plant cell wall polysaccharides and glycoproteins.

To enable biological applications of solid-state NMR spectroscopy, we have developed a wide range of techniques, such as multidimensional correlation techniques, spectral editing techniques, and computational methods for protein resonance assignment; anisotropic-isotropic correlation techniques to measure torsion angles, molecular motion, and conformation-dependent chemical shift tensors; long-distance techniques to determine the oligomeric structures of membrane proteins; and intermolecular correlation techniques to determine the depth of insertion, hydration, and lipid interactions of membrane proteins.

Publications

T. Wang, Y.B. Park, M.A. Caporini, M. Rosay, D.J. Cosgrove and M. Hong, “Sensitivity-enhanced solid-state NMR detection of expansin's target in plant cell walls”, Proc. Natl. Acad. Sci. USA, 110, 16444-9 (2013).

J. K. Williams, D. Tietze, J. Wang, Y. Wu, W.F. DeGrado and M. Hong, “Drug-induced conformational and dynamical changes of the S31N mutant of the influenza M2 proton channel investigated by solid-state NMR”, J. Am. Chem. Soc. 135, 9885-9897 (2013).

F. Hu, K. Schmidt-Rohr and M. Hong, “NMR Detection of pH-Dependent Histidine-Water Proton Exchange Reveals the Conduction Mechanism of a Transmembrane Proton Channel”, J. Am. Chem. Soc. 134, 3703-3713 (2012).

S.D. Cady, K. Schmidt-Rohr, J. Wang, C.S. Soto, W.F. DeGrado, and M. Hong, Structure of the Amantadine Binding Site of Influenza M2 Proton Channels In Lipid Bilayers, Nature, 463, 689-692 (2010).

F. Hu, W. Luo, and M. Hong, “Mechanisms of proton conduction and gating by influenza M2 proton channels from solid-state NMR”, Science, 330, 505-508 (2010).

M. Tang, A. J. Waring and M. Hong, “Phosphate-Mediated Arginine Insertion Into Lipid Membranes and Pore Formation by a Cationic Membrane Peptide from Solid-State NMR”, J. Am. Chem. Soc. 129, 11438-11446 (2007).

R. Mani, S.D. Cady, M. Tang, A.J. Waring, R.I. Lehrer, and M. Hong, Membrane-dependent oligomeric structure and pore formation of a β-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR”, Proc. Natl. Acad. Sci. U.S.A., 103, 16242-16247 (2006).