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Suppression of Diagonal Peaks in Three-Dimensional Protein NMR TROSY-Type HCCH Correlation Experiments

✍ Scribed by Axel Meissner; Ole Winneche Sørensen

Publisher
Elsevier Science
Year
2000
Tongue
English
Weight
114 KB
Volume
144
Category
Article
ISSN
1090-7807

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✦ Synopsis

A novel method for suppression of 13 C-13 C diagonal peaks without sensitivity loss in three-dimensional HCCH TROSY-type NMR correlation experiments involving aromatic side chains in proteins (Pervushin et al., J. Am. Chem. Soc. 120, 6394 -6400 (1998)) is presented. The key element is a spin-state-selective filter in the 13 C-13 C mixing sequence with the dual effect of selecting the TROSY resonance in the preceding evolution period and interchanging TROSY and anti-TROSY resonances. The cross peaks are invariant to this filter but diagonal peak coherence gets concentrated on the anti-TROSY transition so that it can be eliminated by a 13 C 3 1 H TROSY transfer element. The new method is demonstrated using a 13 C, 15 N-labeled protein sample, RAP 18-112 (N-terminal domain of ␣ 2 -macroglobulin receptor associated protein), at 750 MHz.

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