dc.contributor.author | Wong, Alan | |
dc.contributor.author | Beevers, Andrew J. | |
dc.contributor.author | Kukol, A. | |
dc.contributor.author | Dupree, Ray | |
dc.contributor.author | Smith, Mark E. | |
dc.date.accessioned | 2012-01-03T15:01:27Z | |
dc.date.available | 2012-01-03T15:01:27Z | |
dc.date.issued | 2008-05 | |
dc.identifier.citation | Wong , A , Beevers , A J , Kukol , A , Dupree , R & Smith , M E 2008 , ' Solid-state O-17 NMR spectroscopy of a phospholemman transmembrane domain protein : Implications for the limits of detecting dilute 170 sites in biomaterials ' , Solid State Nuclear Magnetic Resonance , vol. 33 , no. 4 , pp. 72-75 . https://doi.org/10.1016/j.ssnmr.2008.04.003 | |
dc.identifier.issn | 0926-2040 | |
dc.identifier.uri | http://hdl.handle.net/2299/7561 | |
dc.description.abstract | The O-17-'diluted' glycine-14 sites in a phospholemman (PLM) transmembrane domain protein are characterized by solid-state O-17 NMR spectroscopy. The PLM transmembrane domain is an a-helical tetramer unit of four 28-residue peptides and is rigidly embedded in a bilayer where each a-helix has an average tilt of 7.3 degrees against the membrane normal. The PLM sample investigated here consists of a high lipid/peptide molar ratio (25: 1) with one glycine residue in each helix enriched to < 40% O-17; thus, this is a very dilute 17 -sample and is the most dilute O-17-membrane protein to date to be characterized by solid-state 17 0 NMR spectroscopy. Based on the spectral analysis of O-17 magic angle spinning (MAS) at 14.1 and 18.8T, the PLM transmembrane domain protein consists of multiple crystallographic gly14 sites, suggesting that the tetramer protein is an asymmetric unit with either C-2- or C-1-rotational symmetry along the bilayer normal. | en |
dc.format.extent | 4 | |
dc.language.iso | eng | |
dc.relation.ispartof | Solid State Nuclear Magnetic Resonance | |
dc.subject | O-17 MAS | |
dc.subject | dilute O-17 content | |
dc.subject | transmembrane protein | |
dc.subject | phospholemman | |
dc.title | Solid-state O-17 NMR spectroscopy of a phospholemman transmembrane domain protein : Implications for the limits of detecting dilute 170 sites in biomaterials | 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 | 10.1016/j.ssnmr.2008.04.003 | |
rioxxterms.type | Journal Article/Review | |
herts.preservation.rarelyaccessed | true | |