M
Mei Hong
Researcher at Massachusetts Institute of Technology
Publications - 256
Citations - 14654
Mei Hong is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: Lipid bilayer & Nuclear magnetic resonance spectroscopy. The author has an hindex of 64, co-authored 240 publications receiving 12628 citations. Previous affiliations of Mei Hong include University of Massachusetts Amherst & University of California, Los Angeles.
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Journal ArticleDOI
Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers
TL;DR: Solid-state NMR spectroscopy indicates that amantadine physically occludes the M2 channel, thus paving the way for developing new antiviral drugs against influenza viruses and demonstrates the ability of solid- state NMR to elucidate small-molecule interactions with membrane proteins and determine high-resolution structures of their complexes.
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Structure and interactions of plant cell-wall polysaccharides by two- and three-dimensional magic-angle-spinning solid-state NMR.
TL;DR: The results suggest that load bearing in plant CWs is accomplished by a single network of all three types of polysaccharides instead of a cellulose-xyloglucan network, thus revising the existing paradigm of CW structure.
Journal ArticleDOI
Mechanisms of Proton Conduction and Gating in Influenza M2 Proton Channels from Solid-State NMR
Fanghao Hu,Wenbin Luo,Mei Hong +2 more
TL;DR: Solid-state nuclear magnetic resonance spectroscopy was used to determine the structure and functional dynamics of the pH-sensing and proton-selective histidine-37 in M2 bound to a cholesterol-containing virus-envelope-mimetic membrane so as to better understand the proton conduction mechanism.
Journal ArticleDOI
De novo design of a transmembrane Zn2+-transporting four-helix bundle.
Nathan H. Joh,Tuo Wang,Manasi P. Bhate,Rudresh Acharya,Yibing Wu,Michael Grabe,Mei Hong,Gevorg Grigoryan,William F. DeGrado +8 more
TL;DR: A membrane-spanning, four-helical bundle that transports first-row transition metal ions Zn2+ and Co2+, but not Ca2+, across membranes is reported, which illustrates the feasibility of designing membrane proteins with predefined structural and dynamic properties.
Journal ArticleDOI
Structure and drug binding of the SARS-CoV-2 envelope protein transmembrane domain in lipid bilayers.
Venkata S. Mandala,Matthew J. McKay,Alexander A. Shcherbakov,Aurelio J. Dregni,Antonios Kolocouris,Mei Hong +5 more
TL;DR: The structure and the drug-binding site of E’s transmembrane domain (ETM), determined using solid-state NMR spectroscopy, sets the stage for designing E inhibitors as antiviral drugs.