Show simple item record

dc.contributor.authorKukol, A.
dc.contributor.authorArkin, I.T.
dc.date.accessioned2011-10-18T10:01:13Z
dc.date.available2011-10-18T10:01:13Z
dc.date.issued2000-02-11
dc.identifier.citationKukol , A & Arkin , I T 2000 , ' Structure of the Influenza C virus CM2 protein transmembrane domain obtained by site-specific infrared dichroism and global molecular dynamics searching ' , Journal of Biological Chemistry , vol. 275 , no. 6 , pp. 4225-4229 . https://doi.org/10.1074/jbc.275.6.4225
dc.identifier.issn0021-9258
dc.identifier.urihttp://hdl.handle.net/2299/6695
dc.descriptionFull text of this article is not available in the UHRA
dc.description.abstractThe 115-residue protein CM2 from Influenza C virus has been recently characterized as a tetrameric integral membrane glycoprotein. infrared spectroscopy and site-directed infrared dichroism were utilized here to determine its transmembrane structure. The transmembrane domain of CM2 is cy-helical, and the helices are tilted by beta = (14.6 +/- 3.0)degrees from the membrane normal. The rotational pitch angle about the helix axis omega for the 1-C-13-labeled residues Gly(59) and Leu(66) is omega = (218 +/- 17)degrees, where w is defined as zero for a residue pointing in the direction of the helix tilt. A detailed structure was obtained from a global molecular dynamics search utilizing the orientational data as an energy refinement term. The structure consists of a left-handed coiled-coil with a helix crossing angle of Omega = 16 degrees, The putative transmembrane pore is occluded by the residue Met(65). In addition hydrogen/deuterium exchange experiments show that the core is not accessible to water.en
dc.format.extent5
dc.language.isoeng
dc.relation.ispartofJournal of Biological Chemistry
dc.subjectB VIRUS
dc.subjectCONFORMATIONAL-CHANGES
dc.subjectSECONDARY STRUCTURE
dc.subjectRNA SEGMENT-6
dc.subjectION CHANNELS
dc.subjectNB
dc.subjectBACTERIORHODOPSIN
dc.subjectSELECTIVITY
dc.subjectM-2
dc.titleStructure of the Influenza C virus CM2 protein transmembrane domain obtained by site-specific infrared dichroism and global molecular dynamics searchingen
dc.contributor.institutionSchool of Life and Medical Sciences
dc.contributor.institutionBiosciences Research Group
dc.contributor.institutionCentre for Research in Mechanisms of Disease and Drug Discovery
dc.contributor.institutionDepartment of Clinical, Pharmaceutical and Biological Science
dc.contributor.institutionCentre for Future Societies Research
dc.description.statusPeer reviewed
rioxxterms.versionofrecord10.1074/jbc.275.6.4225
rioxxterms.typeJournal Article/Review
herts.preservation.rarelyaccessedtrue


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record