A number of heteronuclear 3D techniques have been de-constant-time period of 26-28 ms [2l / 2T(CO)] follows, veloped in recent years to obtain the complete assignment which allows optimum refocusing of the Ca, Cb coupling of 15 N, 13 C-labeled proteins (1). An experiment that often and also allows t
✦ LIBER ✦
A Three-Dimensional NMR Experiment for the Separation of Aliphatic Carbon Chemical Shifts via the Carbonyl Chemical Shift in 15N, 13C-Labeled Proteins
✍ Scribed by L.E. Kay
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 319 KB
- Volume
- 101
- Category
- Article
- ISSN
- 1064-1866
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
A New Three-Dimensional Pulse Sequence f
✍
Renzo Bazzo; Daniel O. Cicero; Gaetano Barbato
📂
Article
📅
1996
🏛
Elsevier Science
🌐
English
⚖ 90 KB
NMR chemical shift mapping of the bindin
✍
Jikui Song; John L. Markley
📂
Article
📅
2001
🏛
John Wiley and Sons
🌐
English
⚖ 201 KB
## Abstract The substrate‐like inhibition of serine proteinases by avian ovomucoid domains has provided an excellent model for protein inhibitor‐proteinase interactions of the standard type. ^1^H,^15^N and ^13^C NMR studies have been undertaken on complexes formed between turkey ovomucoid third dom