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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

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.

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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: Article
Journal or Publication Title: Solid State Nuclear Magnetic Resonance
Uncontrolled Keywords: O-17 MAS, dilute O-17 content, transmembrane protein, phospholemman
Subjects: UNSPECIFIED
Departments: VC's Office
ID Code: 52845
Deposited By: ep_importer_pure
Deposited On: 29 Feb 2012 09:02
Refereed?: Yes
Published?: Published
Last Modified: 09 Apr 2014 23:09
Identification Number:
URI: http://eprints.lancs.ac.uk/id/eprint/52845

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