A set of BEST triple-resonance experiments for time-optimized protein resonance assignment.
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.
Lescop
Ewen
E
Institut 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.
Schanda
Paul
P
Brutscher
Bernhard
B
D000465:Algorithms; D009682:Magnetic Resonance Spectroscopy / Q000706:statistics & numerical data*; D015233:Models, Statistical; D011506:Proteins / Q000737:chemistry*; D025801:Ubiquitin / Q000737:chemistry
D011506:Proteins; D025801:Ubiquitin