NMR detection of side chain–side chain hydrogen bonding interactions in 13C/15N-labeled proteins
✍ Scribed by Aizhuo Liu; Weidong Hu; Ananya Majumdar; Michael K. Rosen; Dinshaw J. Patel
- Book ID
- 110263520
- Publisher
- Springer Netherlands
- Year
- 2000
- Tongue
- English
- Weight
- 96 KB
- Volume
- 17
- Category
- Article
- ISSN
- 0925-2738
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As aromatic residues very often are part of the hydrophobic essential for an accurate and precise structure determination. core of proteins, the unambiguous assignment of the aromatic Therefore, methods for the unambiguous assignment of aroproton resonances is essential for an accurate and precise s
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
Complete resonance assignments are mandatory for de-will refer to as (HB)CB(CG)CDHD. Finally, the assigned side-chain resonances are linked to the backbone by use of tailed NMR studies of protein structures in solution. In many proteins, aromatic residues are involved in the construction an (H)CCH-C
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