A powerful method of sequential proton resonance assignment in proteins using relayed 15N-1H multiple quantum coherence spectroscopy.
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.
Gronenborn
A M
AM
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD 20892.
Bax
A
A
Wingfield
P T
PT
Clore
G M
GM
D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D009584:Nitrogen; D011487:Protein Conformation; D011506:Proteins; D011522:Protons; D011789:Quantum Theory
D011506:Proteins; D011522:Protons; D006859:Hydrogen; D009584:Nitrogen