We describe an approach to efficiently determine the backbone conformation of solid proteins that utilizes selective and extensive (13)C labeling in conjunction with two-dimensional magic-angle-spinning NMR. The selective (13)C labeling approach aims to reduce line broadening and other multispin com
✦ LIBER ✦
Torsion Angle Determination in Solid 13 C-Labeled Amino Acids and Peptides by Separated-Local-Field Double-Quantum NMR
✍ Scribed by Schmidt-Rohr, K.
- Book ID
- 126305736
- Publisher
- American Chemical Society
- Year
- 1996
- Tongue
- English
- Weight
- 158 KB
- Volume
- 118
- Category
- Article
- ISSN
- 0002-7863
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We demonstrate a dipolar-chemical shift correlation technique for sign-sensitive determination of the torsion angle in solid peptides and proteins under magic-angle spinning. The indirect dimension of the experiment is obtained by separate but synchronous evolution of the magnetization under the 15