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
✦ LIBER ✦
The use of1JCαHαcoupling constants as a probe for protein backbone conformation
✍ Scribed by Geerten W. Vuister; Frank Delaglio; Ad Bax
- Book ID
- 104679444
- Publisher
- Springer Netherlands
- Year
- 1993
- Tongue
- English
- Weight
- 838 KB
- Volume
- 3
- Category
- Article
- ISSN
- 0925-2738
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## Abstract It is demonstrated that in a case where neither the proton nor the natural‐abundance ^13^C‐satellite spectra of a partially oriented molecule carry enough structural information, one can determine the entire molecular geometry by the combined use of several liquid crystals as solvents.