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
Assignment of Side-Chain 13C Resonances in Perdeuterated Proteins
β Scribed by Farmer, Bennett T.; Venters, Ronald A.
- Book ID
- 125959415
- Publisher
- American Chemical Society
- Year
- 1995
- Tongue
- English
- Weight
- 834 KB
- Volume
- 117
- Category
- Article
- ISSN
- 0002-7863
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π SIMILAR VOLUMES
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
Two 3D experiments, (H)CCH 3 -TOCSY and H(C)CH 3 -TOCSY, are proposed for resonance assignment of methyl-containing amino acid side chains. After the initial proton-carbon INEPT step, during which either carbon or proton chemical shift labeling is achieved (t 1 ), the magnetization is spread along t