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Three-dimensional solid-state NMR spectroscopy of a peptide oriented in membrane bilayers

Journal of Biomolecular NMR volume 6, pages 329–334 (1995)Cite this article

Summary

A three-dimensional 1H chemical shift/1H-15N dipolar coupling/15N chemical shift correlation spectrum was obtained on a sample of specifically 15N-labeled magainin peptides oriented in lipid bilayers between glass plates in a flat-coil probe. The spectrum showed complete resolution of the resonances from two labeled amide sites in all three dimensions. The three orientationally dependent frequencies associated with each resonance enabled the orientation of the peptide planes to be determined relative to the direction of the applied magnetic field. These results demonstrate the feasibility of multiple-pulse spectroscopy in a flat-coil probe, the ability to measure three spectral parameters from each site in a single experiment, and the potential for resolving among many labeled sites in oriented membrane proteins.

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Affiliations

  1. Department of Chemistry, University of Pennsylvania, 231 South 34th Street, 19104, Philadelphia, PA, USA

    A. Ramamoorthy, F. M. Marassi & S. J. Opella

  2. Magainin Pharmaceuticals, 5110 Campus Drive, 19462, Plymouth Meeting, PA, USA

    M. Zasloff

Authors
  1. A. Ramamoorthy
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  2. F. M. Marassi
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  3. M. Zasloff
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  4. S. J. Opella
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Ramamoorthy, A., Marassi, F.M., Zasloff, M. et al. Three-dimensional solid-state NMR spectroscopy of a peptide oriented in membrane bilayers. J Biomol NMR 6, 329–334 (1995). https://doi.org/10.1007/BF00197814

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  • DOI: https://doi.org/10.1007/BF00197814

Key words

  • Solid-state NMR
  • Magainin
  • Membranes
  • Oriented samples
  • Structure determination