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
Heteronuclear two-and three-dimensional nmr spectroscopy of 13C in natural abundance by multiplicity selection and editing: Application to peptides
✍ Scribed by H. Kessler; P. Schmieder
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1991
- Tongue
- English
- Weight
- 503 KB
- Volume
- 31
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
Several new proton‐detected heteronuclear two‐dimensional (2D) nmr techniques are presented that exhibit the features of selection and editing of multiplicity. The theoretical basis of the new features is briefly discussed and the application of the 2D techniques to a thioanalogon of Cyclosporin A [Thio‐(1)‐cyclosporin A] is shown. In addition, an extension of the experiments to three‐dimensional (3D) techniques is demonstrated and the application of two 3D techniques to Thio‐(1)‐cyclosporin A with ^13^C in natural abundance is presented. The new techniques can help simplify heteronuclear shift correlations and increase the resolution in the carbon dimension.
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