Wong, Alan and Beevers, Andrew J. and Kukol, Andreas and 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, 33 (4). pp. 72-75. ISSN 1527-3326Full text not available from this repository.
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.
|Journal or Publication Title:||Solid State Nuclear Magnetic Resonance|
|Uncontrolled Keywords:||O-17 MAS, dilute O-17 content, transmembrane protein, phospholemman|
|Deposited On:||29 Feb 2012 09:02|
|Last Modified:||30 Mar 2016 01:18|
Actions (login required)