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Updated: Jul 15, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
A set of BEST triple-resonance experiments for time-optimized protein resonance assignment
Ewen Lescop1, Paul Schanda, Bernhard Brutscher
1Institut de Biologie Structurale, Jean-Pierre Ebel Centre National de la Recherche Scientifique-Commissariat à l'Energie Atomique-UJF, 41 rue Jules Horowitz, 38027 Grenoble Cedex, France.
Abstract:
A series of sequential, intra-residue, and bi-directional BEST H-N-CA, H-N-CO, and H-N-CB pulse sequences is presented that extends the BEST concept introduced recently for fast multidimensional protein NMR [Schanda et al., J. Am. Chem. Soc. 128 (2006) 9042] to the complete set of experiments required for sequential resonance assignment. We demonstrate for the protein ubiquitin that 3D BEST H-N-C correlation spectra can be recorded on a 600MHz NMR spectrometer equipped with a cryogenic probe in only a few minutes of acquisition time with sufficient sensitivity to detect all expected cross peaks.
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