期刊论文详细信息
FEBS Letters
Long‐range 15N‐1H correlation as an aid to sequential proton resonance assignment of proteins Application to the DNA‐binding protein ner from phage Mu
Bax, Ad1  Wingfield, Paul2  Clore, G.Marius1  Gronenborn, Angela M.1 
[1] Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA;Glaxo Institute for Molecular Biology SA, 46 Route des Acacias, CH-1211, Geneva, Switzerland
关键词: NMR;    Sequential resonance assignment;    15N labeling;    Heteronuclear multiple bond correlation;    ner protein;    Phage Mu;    HMBC;    1H-detected heteronuclear multiplebond correlation spectroscopy;    HMQC;    1H-detected heteronuclear multiple quantum coherence spectroscopy;    COSY;    homonuclear correlated spectroscopy;    NOESY;    homonuclear nuclear Overhauser enhancement spectroscopy;    HOHAHA;    homonuclear Hartmann-Hahn spectroscopy;   
DOI  :  10.1016/0014-5793(88)80216-3
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

A method is described for sequential resonance assignment of protein 1H-NMR spectra relying on the detection of long-range correlations between 15N and CαH atoms using 1H-detected heteronuclear multiple-bond correlation spectroscopy. In particular, the observation of the two-bond 15N(i)-CαH(i) and three-bond 15N(i)-CαH(i−1) correlations enables one to connect one residue with the next. Because the magnitude of the long-range couplings is small (<6 Hz), the sensitivity of this experiment is necessarily low and requires the use of 15N-enriched protein samples. Further, because the size of the 15N(i)-CαH(i−1) coupling is very sensitive to the ψ backbone torsion angle, structural information can be derived. The application of this experiment is illustrated with the 75-residue DNA-binding protein ner from phage Mu.

【 授权许可】

Unknown   

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