A simple one-dimensional solid-state NMR method to characterize the nuclear spin interaction tensors associated with the peptide bond

J Magn Reson. 1998 Jul;133(1):204-6. doi: 10.1006/jmre.1998.1442.

Abstract

We propose a simple one-dimensional RF pulse sequence for the study of chemical shift and heteronuclear dipolar coupling tensors of oriented as well as unoriented solids. An off-resonance RF decoupling of protons during the signal acquisition of less sensitive nuclei is used to suppress homonuclear 1H-1H dipolar interactions. This method is experimentally demonstrated on peptide samples selectively labeled with 15N isotope.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Algorithms
  • Electron Spin Resonance Spectroscopy*
  • Hydrogen / chemistry
  • Hydrogen Bonding
  • Magnetic Resonance Spectroscopy / methods*
  • Magnetics
  • Nitrogen Isotopes
  • Peptides / chemistry*
  • Protons
  • Radio Waves
  • Signal Processing, Computer-Assisted
  • Valine / analogs & derivatives
  • Valine / chemistry

Substances

  • Nitrogen Isotopes
  • Peptides
  • Protons
  • Hydrogen
  • Valine
  • N-acetylvaline