## Abstract The ^15^N^13^C coupling constants in ^15^N labelled azaadamantane have been measured and interpreted in terms of their conformational dependence as compared with ^15^N‐quinuclidine.
Improved pulse sequences for measuring coupling constants in13C,15N-labeled proteins
✍ Scribed by Jens Chr. Madsen; Ole Winneche Sørensen; Poul Sørensen; Flemming M. Poulsen
- Publisher
- Springer Netherlands
- Year
- 1993
- Tongue
- English
- Weight
- 297 KB
- Volume
- 3
- Category
- Article
- ISSN
- 0925-2738
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
Sensitive three-dimensional NMR experiments, based on the E.COSY principle, are presented for the measurement of the 3J(HN, H~) and 3J(HN,C') coupling constants in uniformly 13C-and 15N-labeled proteins. They employ gradient coherence selection in combination with the sensitivity enhancement method
A set of three improved two-dimensional (2D) NMR methods for measuring one-bond 15 N-1 H coupling constants in the protein backbone is presented. They are tailored to suit the size of the TROSY effect, i.e., the degree of interference between dipolar and chemical shift anisotropy relaxation mechanis
Complete resonance assignments are mandatory for de-will refer to as (HB)CB(CG)CDHD. Finally, the assigned side-chain resonances are linked to the backbone by use of tailed NMR studies of protein structures in solution. In many proteins, aromatic residues are involved in the construction an (H)CCH-C
A triple-resonance pulse sequence is presented for the quantitative measurement of 1 H ␣ -13 C ␣ single-bond couplings in 15 N, 13 C uniformly labeled proteins. This 1 J CH -modulated (HACACO)NH experiment yields 1 H N -15 N-correlated 2D spectra in which the amplitude of each peak is modulated by t