Efficient resonance assignment of proteins in MAS NMR by simultaneous intra- and inter-residue 3D correlation spectroscopy

J Biomol NMR. 2013 Mar;55(3):257-65. doi: 10.1007/s10858-013-9707-0. Epub 2013 Jan 19.


Resonance assignment is the first step in NMR structure determination. For magic angle spinning NMR, this is typically achieved with a set of heteronuclear correlation experiments (NCaCX, NCOCX, CONCa) that utilize SPECIFIC-CP (15)N-(13)C transfers. However, the SPECIFIC-CP transfer efficiency is often compromised by molecular dynamics and probe performance. Here we show that one-bond ZF-TEDOR (15)N-(13)C transfers provide simultaneous NCO and NCa correlations with at least as much sensitivity as SPECIFIC-CP for some non-crystalline samples. Furthermore, a 3D ZF-TEDOR-CC experiment provides heteronuclear sidechain correlations and robustness with respect to proton decoupling and radiofrequency power instabilities. We demonstrate transfer efficiencies and connectivities by application of 3D ZF-TEDOR-DARR to a model microcrystalline protein, GB1, and a less ideal system, GvpA in intact gas vesicles.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

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


  • Carbon Isotopes
  • Nitrogen Isotopes
  • Proteins