Side-chain carbon resonance assignments are difficult to obtain for larger proteins. While standard methods require protons for excitation and detection of magnetization, their presence is often unacceptable and often leads to unacceptable relaxation losses at the directly bound carbon sites. In thi
Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR
โ Scribed by Grzesiek, Stephan; Bax, Ad
- Book ID
- 118127035
- Publisher
- American Chemical Society
- Year
- 1992
- Tongue
- English
- Weight
- 380 KB
- Volume
- 114
- Category
- Article
- ISSN
- 0002-7863
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
We thank Claude Klee for help and encouragement in our study of calcineurin B, Hao Ren for protein expression, and Marius Clore and Dennis Torchia for useful discussions. This work was supported by the AIDS Targeted Anti-Viral Program of the Office of the Director of the National Institutes of Healt
A 3D triple resonance experiment has been designed to provide intraresidual and sequential correlations between amide nitrogens and c~-carbons in uniformly 13C/15N-labeled proteins. In-phase 13C~ magnetization is transferred to the aliphatic side-chain protons via the side-chain carbons using a CC-T