An earlier two-dimensional NOESY experiment with diagonal peak suppression in the 1 H N -1 H N region is extended to three dimensions by including 15 N evolution while maintaining the TROSY approach throughout. The technique suppresses all anti-TROSY resonances by appropriate pulse sequence elements
Suppression of Diagonal Peaks in TROSY-Type 1H NMR NOESY Spectra of 15N-Labeled Proteins
✍ Scribed by Axel Meissner; Ole Winneche Sørensen
- Publisher
- Elsevier Science
- Year
- 1999
- Tongue
- English
- Weight
- 86 KB
- Volume
- 140
- Category
- Article
- ISSN
- 1090-7807
No coin nor oath required. For personal study only.
✦ Synopsis
A novel method for suppression of diagonal peaks in the amide region of NOESY NMR spectra of 15 N-labeled proteins is presented. The method is particularly useful for larger proteins at high magnetic fields where interference between dipolar and chemical shift anisotropy relaxation mechanisms results in large TROSY effects, i.e., large differences in 1 H N linewidths depending on the spin state of attached 15 N nuclei. In this limit the new TROSY NOESY method does not compromise sensitivity. It is demonstrated using a perdeuterated 15 N-labeled protein sample, Neural Cell Adhesion Molecule 213-308 (NCAM) from rat, in H 2 O at 800 MHz.
📜 SIMILAR VOLUMES
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-s