Journal
JOURNAL OF BIOMOLECULAR NMR
Volume 55, Issue 3, Pages 257-265Publisher
SPRINGER
DOI: 10.1007/s10858-013-9707-0
Keywords
3D MAS NMR; TEDOR; DARR; Sidechain-backbone correlation
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Funding
- National Institute of Biomedical Imaging and Bioengineering of the National Institutes of Health [EB001035, EB-001960, EB-002926]
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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 N-15-C-13 transfers. However, the SPECIFIC-CP transfer efficiency is often compromised by molecular dynamics and probe performance. Here we show that one-bond ZF-TEDOR N-15-C-13 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.
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