Triple resonance MAS NMR with (13C, 15N) labelled molecules: reduced dimensionality data acquisition via 13C-15N heteronuclear two-spin coherence transfer pathways

J Biomol NMR. 2004 Feb;28(2):185-90. doi: 10.1023/B:JNMR.0000013834.36262.79.

Abstract

A reduced dimensionality magic angle spinning solid-state NMR experimental protocol for obtaining chemical shift correlation spectra of dipolar coupled nuclei in uniformly ((13)C, (15)N) labelled biological systems is described and demonstrated. The method involves a mapping of the evolution frequencies of heteronuclear (13)C-(15)N zero- and double-quantum coherences. In comparison to a reduced dimensionality procedure involving the simultaneous incrementation of two single-quantum chemical shift evolution periods, the approach described here could be potentially advantageous for minimising the heat dissipated in the probe by high power (1)H decoupling in experiments requiring long t (1) acquisition times.

MeSH terms

  • Carbon Isotopes
  • Nitrogen Isotopes
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Proteins / chemistry

Substances

  • Carbon Isotopes
  • Nitrogen Isotopes
  • Proteins