Related Experiment Video
Updated: May 15, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Efficient resonance assignment of proteins in MAS NMR by simultaneous intra- and inter-residue 3D correlation
Eugenio Daviso1, Matthew T Eddy, Loren B Andreas
1Department of Chemistry, Brandeis University, Waltham, MA 02454-9110, USA.
Abstract:
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.
Related Concept Videos
2D NMR: Overview of Homonuclear Correlation Techniques
COSY90 is the standard two-dimensional (2D) COSY experiment that...
2D NMR: Overview of Heteronuclear Correlation Techniques
2D NMR: Homonuclear Correlation Spectroscopy (COSY)
2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)
Double Resonance Techniques: Overview
Spin decoupling is usually achieved by...
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution
