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

FEBS Letters

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.

【 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 C^αH atoms using ¹H-detected heteronuclear multiple-bond correlation spectroscopy. In particular, the observation of the two-bond ¹⁵N(i)-C^αH(i) and three-bond ¹⁵N(i)-C^αH(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)-C^αH(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