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
Correlation of Backbone Amide and Aliphatic Side-Chain Resonances in 13C/15N-Enriched Proteins by Isotropic Mixing of 13C Magnetization
β Scribed by S. Grzesiek; J. Anglister; A. Bax
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 389 KB
- Volume
- 101
- Category
- Article
- ISSN
- 1064-1866
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β¦ Synopsis
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 Health.
π SIMILAR VOLUMES
Recently, a novel three-dimensional, triple-resonance ex-respect to the nitrogen, which then evolves into in-phase periment was described which correlates intraresidue 13 CO, carbonyl magnetization again. Evolution under the 1 J CaCO 13
HCN, a new 3D NMR technique for stepwise coherence transfer rarely sufficient to establish the mechanism through which from 1 H to 13 C to 15 N and reverse through direct spin couplings it participates in the protein's function. The structure may 1 J CH and 1 J CN , is presented as a method for dete