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Solid-state O-17 NMR spectroscopy of a phospholemman transmembrane domain protein : implications for the limits of detecting dilute 170 sites in biomaterials
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Wong, A. (Alan), Beevers, Andrew J., Kukol, Andreas, Dupree, Ray and Smith, Mark 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. doi:10.1016/j.ssnmr.2008.04.003 ISSN 0926-2040.
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Official URL: http://dx.doi.org/10.1016/j.ssnmr.2008.04.003
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. (c) 2008 Elsevier Inc. All rights reserved.
Item Type: | Journal Article | ||||
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Subjects: | Q Science > QD Chemistry | ||||
Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry Faculty of Science, Engineering and Medicine > Science > Physics Administration > University Executive Office |
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Library of Congress Subject Headings (LCSH): | Proteins, Nuclear magnetic resonance spectroscopy | ||||
Journal or Publication Title: | Solid State Nuclear Magnetic Resonance | ||||
Publisher: | Academic Press | ||||
ISSN: | 0926-2040 | ||||
Official Date: | May 2008 | ||||
Dates: |
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Volume: | Vol.33 | ||||
Number: | No.4 | ||||
Number of Pages: | 4 | ||||
Page Range: | pp. 72-75 | ||||
DOI: | 10.1016/j.ssnmr.2008.04.003 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Restricted or Subscription Access | ||||
Funder: | Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC) | ||||
Grant number: | BB/C000471/1 (BBSRC) |
Data sourced from Thomson Reuters' Web of Knowledge
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