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dc.contributor.authorElkins, Matthew Ryan
dc.contributor.authorHong, Mei
dc.date.accessioned2020-08-25T15:08:22Z
dc.date.available2020-08-25T15:08:22Z
dc.date.issued2019-08
dc.identifier.issn0959-440X
dc.identifier.urihttps://hdl.handle.net/1721.1/126796
dc.description.abstractMagic-angle-spinning (MAS) solid-state NMR spectroscopy is a versatile technique to elucidate functionally important protein–ligand interactions in lipid membranes. Here, we review recent solid-state NMR studies of membrane protein interactions with cholesterol, lipids, transported substrates, and peptide ligands. These studies are conducted in synthetic or native lipid bilayers to provide an accurate environment for ligand binding. The solid-state NMR approaches include multinuclear detection to gain comprehensive structural information, distance measurements to locate ligand-binding sites, and dynamic nuclear polarization and 1 H detection to enhance spectral sensitivity. These studies provide novel insights into the mechanisms of virus budding, virus entry into cells, transmembrane signaling, substrate transport, antibacterial action, and many other biological processes.en_US
dc.description.sponsorshipNational Institutes of Health (U.S.) (Grant GM088204)en_US
dc.language.isoen
dc.publisherElsevier BVen_US
dc.relation.isversionof10.1016/J.SBI.2019.02.002en_US
dc.rightsCreative Commons Attribution-NonCommercial-NoDerivs Licenseen_US
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/en_US
dc.sourcePMCen_US
dc.titleElucidating ligand-bound structures of membrane proteins using solid-state NMR spectroscopyen_US
dc.typeArticleen_US
dc.identifier.citationElkins, Matthew R. and Mei Hong. “Elucidating ligand-bound structures of membrane proteins using solid-state NMR spectroscopy.” Current Opinion in Structural Biology, 57 (August 2019): 103–109 © 2019 The Author(s)en_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Chemistryen_US
dc.relation.journalCurrent Opinion in Structural Biologyen_US
dc.eprint.versionAuthor's final manuscripten_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dc.date.updated2020-08-24T13:19:47Z
dspace.date.submission2020-08-24T13:19:49Z
mit.journal.volume57en_US
mit.licensePUBLISHER_CC


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