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Susceptibility corrections in solid-state NMR experiments with oriented membrane samples. Part I: applications.

Ralf W Glaser1, Anne S Ulrich

  • 1Institute of Molecular Biology, Friedrich-Schiller-Universität Jena, Winzerlaer Str. 10, D-07745 Jena, Germany.

Journal of Magnetic Resonance (San Diego, Calif. : 1997)
|August 23, 2003
PubMed
Summary

Accurate chemical shift referencing in solid-state NMR is crucial for studying membrane proteins. New methods using isotropic references or lipid signals improve precision, revealing peptide orientation changes in membranes.

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Area of Science:

  • Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy
  • Biophysics
  • Materials Science

Background:

  • Solid-state NMR experiments on oriented membranes require compensation for magnetic susceptibility effects due to non-spherical sample shapes.
  • These effects cause significant frequency deviations (up to 10 ppm), impacting nuclei like 1H, 13C, and 19F with narrow chemical shift anisotropy.

Purpose of the Study:

  • To propose and validate new chemical shift referencing schemes for solid-state NMR of oriented membrane samples.
  • To investigate the concentration-dependent membranolytic effect of the antimicrobial peptide PGLa using these referencing methods.

Main Methods:

  • Two referencing schemes were developed: stacking a glass container with an isotropic reference and using the intrinsic proton signal of hydrated lipids.

Related Experiment Videos

  • Experiments were conducted on multilayers of hydrated DMPC with a 19F-labeled peptide, oriented between glass plates at various peptide/lipid ratios.
  • Sample thickness was adjusted (3-18 plates) to maintain a constant peptide amount across different concentrations.

    • Main Results:

    • The proposed referencing schemes effectively compensate for magnetic susceptibility effects, enabling accurate measurements.
    • A small but significant 5 ppm change in the 19F anisotropic chemical shift of PGLa was observed, correlating with changes in peptide orientation and/or dynamics.
    • The study demonstrated the critical role of accurate referencing in revealing subtle structural and dynamic changes in membrane-bound peptides.

    Conclusions:

    • Accurate chemical shift referencing is essential for high-resolution solid-state NMR of oriented membrane systems.
    • The developed methods provide reliable referencing, facilitating the study of membrane protein structure and function.
    • The findings on PGLa provide insights into its membranolytic mechanism and concentration-dependent behavior.