Published in

Elsevier, Solid State Nuclear Magnetic Resonance, 4(33), p. 72-75, 2008

DOI: 10.1016/j.ssnmr.2008.04.003

Links

Tools

Export citation

Search in Google Scholar

Solid-state 17O NMR spectroscopy of a phospholemman transmembrane domain protein: Implications for the limits of detecting dilute 17O sites in biomaterials

Journal article published in 2008 by Alan Wong, Andrew J. Beevers, Andreas Kukol, Ray Dupree ORCID, Mark E. Smith
This paper was not found in any repository, but could be made available legally by the author.
This paper was not found in any repository, but could be made available legally by the author.

Full text: Unavailable

Green circle
Preprint: archiving allowed
Upload
Orange circle
Postprint: archiving restricted
Upload
Red circle
Published version: archiving forbidden
Policy details
Data provided by SHERPA/RoMEO

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