A powerful method of sequential proton resonance assignment in proteins using relayed 15N‐1H multiple quantum coherence spectroscopy

FEBS Letters

Bax, Ad¹  Clore, G.Marius¹  Wingfield, Paul T.²  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-1227 Geneva, Switzerland

关键词: Sequential resonance assignment;    15N labeling;    Relayed multiple quantum coherence spectroscopy;    Protein;    ner;    Phage;    Mu;    NMR;    nuclear magnetic resonance COSY;    homonuclear correlated spectroscopy;    NOESY;    homonuclear nuclear Overhauser enhancement spectroscopy;    HOHAHA;    homonuclear Hartmann-Hahn spectroscopy;    HMQC;    1H-detected heteronuclear multiple quantum coherence spectroscopy;    rf;    radiofrequency;   

DOI  :  10.1016/0014-5793(89)81224-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A powerful method of sequential resonance assignment of protein ¹H-NMR spectra is presented and illustrated with respect to the DNA-binding protein ner from phage Mu. It is based on correlating proton-proton through-space and through-bond connectivities with the chemical shift of the directly bonded ¹⁵N atom. By this means, ambiguities arising from chemical shift degeneracy of amide proton resonances can be resolved. The experiments described involve combining the ¹H-detected heteronuclear multiple quantum coherence correlation experiment with homonuclear nuclear Overhauser enhancement, J-correlated or Hartmann-Hahn experiments.

【 授权许可】

Unknown