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Open seminar

演 題 「Solid State NMR: A Critical Technology for Membrane Protein Structural Biology」
日 時 2014年03月13日(木) 16:00
講演者 Timothy A. Cross 教 授 (Florida state university, National High Magnetic Field Laboratory, US)
場 所

分子科学研究所 研究棟セミナー室 301号室

概 要

Solid state NMR spectroscopy can provide both absolute and relative restraints for the structural characterization of membrane proteins. Absolute restraints, like residual dipolar interactions in solution NMR relate an atomic site in the protein to an alignment tensor, while relative restraints like distance or torsional restraints relative one part of the protein to another part of the protein. Unlike water soluble proteins, membrane proteins must be oriented relative to their environment for their functional role. The combination of orientational restraints (i.e. absolute restraints) in which uniformly aligned lipid bilayer preparations of the proteins are uniformly aligned with respect to the magnetic field and distance restraints permit the three dimensional structural characterization of these proteins. While cryo-EM and X-Ray crystallography have been very successful for the characterization of large helical membrane proteins there has been much less success with small helical membrane proteins having 1-4 transmembrane helices. Solid state NMR has been demonstrated to be an excellent technology for the accurate structural characterization of such proteins. In illustrating this technology I will describe progress towards the structural characterizations of the M2 protein from Influenza A virus, a highly selective proton channel. I will also discuss structural efforts with three membrane proteins from Mycobacterium tuberculosis, CgrA is a regulatory protein in cell division having two transmembrane helices, Rv1861 has three transmembrane helices that binds nucleotides and participates in the regulation of transglycosylase activity, and MgtC is a 6-helix protein that regulates ATP synthase. Through these examples I hope to demonstrate how solid state NMR is indeed a critical tool for membrane protein structural biology.

その他

Prof. Timothy A. 
http://www.magnet.fsu.edu/search/personnel/getprofile.

http://www.fsu.edu/profiles/cross/

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