dc.contributor.author | Kukol, A. | |
dc.contributor.author | Arkin, I.T. | |
dc.date.accessioned | 2011-10-18T10:01:13Z | |
dc.date.available | 2011-10-18T10:01:13Z | |
dc.date.issued | 2000-02-11 | |
dc.identifier.citation | Kukol , 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.issn | 0021-9258 | |
dc.identifier.uri | http://hdl.handle.net/2299/6695 | |
dc.description | Full text of this article is not available in the UHRA | |
dc.description.abstract | The 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.extent | 5 | |
dc.language.iso | eng | |
dc.relation.ispartof | Journal of Biological Chemistry | |
dc.subject | B VIRUS | |
dc.subject | CONFORMATIONAL-CHANGES | |
dc.subject | SECONDARY STRUCTURE | |
dc.subject | RNA SEGMENT-6 | |
dc.subject | ION CHANNELS | |
dc.subject | NB | |
dc.subject | BACTERIORHODOPSIN | |
dc.subject | SELECTIVITY | |
dc.subject | M-2 | |
dc.title | Structure of the Influenza C virus CM2 protein transmembrane domain obtained by site-specific infrared dichroism and global molecular dynamics searching | en |
dc.contributor.institution | School of Life and Medical Sciences | |
dc.contributor.institution | Biosciences Research Group | |
dc.contributor.institution | Centre for Research in Mechanisms of Disease and Drug Discovery | |
dc.contributor.institution | Department of Clinical, Pharmaceutical and Biological Science | |
dc.contributor.institution | Centre for Future Societies Research | |
dc.description.status | Peer reviewed | |
rioxxterms.versionofrecord | 10.1074/jbc.275.6.4225 | |
rioxxterms.type | Journal Article/Review | |
herts.preservation.rarelyaccessed | true | |