3D13C-15N-heteronuclear two-spin coherence spectroscopy for polypeptide backbone assignments in13C-15N-double-labeled proteins
✍ Scribed by Thomas Szyperski; Gerhard Wider; John H. Bushweller; Kurt Wüthrich
- Book ID
- 104679448
- Publisher
- Springer Netherlands
- Year
- 1993
- Tongue
- English
- Weight
- 332 KB
- Volume
- 3
- Category
- Article
- ISSN
- 0925-2738
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
In principle, the relaxation of any proton ( 1 H ) , carbon carbon ( 13 C) relaxation in a 13 C, 15 N-doubly enriched sample ( 13 C ) , or nitrogen ( 15 N ) spin in a protein will contain of the thermostable Sso7d protein have been investigated. Pulse information about dynamics. The most common appl
A ''Double-WURST'' decoupling sequence is constructed for sitogether with suitable phase cycles, mainly to compensate multaneously decoupling the 13 CO and 13 C a regions in 15 N/ 13 C-doupulse imperfections. ## ble-labeled proteins. It uses frequency-shifted WURST decoupling The early design of