Triple resonance MAS NMR with (13C, 15N) labelled molecules: reduced dimensionality data acquisition via 13C-15N heteronuclear two-spin coherence transfer pathways.
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.
Leppert
Jörg
J
Abteilung Molekulare Biophysik/NMR-Spektroskopie, Institut für Molekulare Biotechnologie, 07745 Jena, Germany.
Heise
Bert
B
Ohlenschläger
Oliver
O
Görlach
Matthias
M
Ramachandran
Ramadurai
R
D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011506:Proteins / Q000737:chemistry
D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D011506:Proteins