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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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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; Beevers, Andrew J.; Kukol, Andreas; Dupree, Ray; Smith, Mark E.

In: Solid State Nuclear Magnetic Resonance, Vol. 33, No. 4, 01.05.2008, p. 72-75.

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Wong, Alan ; Beevers, Andrew J. ; Kukol, Andreas ; Dupree, Ray ; Smith, Mark E. / Solid-state O-17 NMR spectroscopy of a phospholemman transmembrane domain protein: Implications for the limits of detecting dilute 170 sites in biomaterials. In: Solid State Nuclear Magnetic Resonance. 2008 ; Vol. 33, No. 4. pp. 72-75.

Bibtex

@article{13e265e495d14ffa80ce8699afe28554,
title = "Solid-state O-17 NMR spectroscopy of a phospholemman transmembrane domain protein: Implications for the limits of detecting dilute 170 sites in biomaterials",
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.",
keywords = "O-17 MAS, dilute O-17 content, transmembrane protein, phospholemman",
author = "Alan Wong and Beevers, {Andrew J.} and Andreas Kukol and Ray Dupree and Smith, {Mark E.}",
year = "2008",
month = may,
day = "1",
doi = "10.1016/j.ssnmr.2008.04.003",
language = "English",
volume = "33",
pages = "72--75",
journal = "Solid State Nuclear Magnetic Resonance",
issn = "0926-2040",
publisher = "ACADEMIC PRESS INC ELSEVIER SCIENCE",
number = "4",

}

RIS

TY - JOUR

T1 - Solid-state O-17 NMR spectroscopy of a phospholemman transmembrane domain protein: Implications for the limits of detecting dilute 170 sites in biomaterials

AU - Wong, Alan

AU - Beevers, Andrew J.

AU - Kukol, Andreas

AU - Dupree, Ray

AU - Smith, Mark E.

PY - 2008/5/1

Y1 - 2008/5/1

N2 - 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.

AB - 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.

KW - O-17 MAS, dilute O-17 content, transmembrane protein, phospholemman

U2 - 10.1016/j.ssnmr.2008.04.003

DO - 10.1016/j.ssnmr.2008.04.003

M3 - Journal article

VL - 33

SP - 72

EP - 75

JO - Solid State Nuclear Magnetic Resonance

JF - Solid State Nuclear Magnetic Resonance

SN - 0926-2040

IS - 4

ER -