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A powerful method of sequential proton resonance assignment in proteins using relayed 15 N‐ 1 H multiple quantum coherence spectroscopy
Author(s) -
Gronenborn Angela M.,
Bax Ad,
Wingfield Paul T.,
Clore G.Marius
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81224-4
Subject(s) - homonuclear molecule , heteronuclear molecule , proton , chemistry , coherence (philosophical gambling strategy) , resonance (particle physics) , nuclear overhauser effect , spectroscopy , nuclear magnetic resonance spectroscopy , nuclear magnetic resonance , degeneracy (biology) , two dimensional nuclear magnetic resonance spectroscopy , spectral line , molecular physics , atomic physics , physics , molecule , quantum mechanics , bioinformatics , organic chemistry , biology
A powerful method of sequential resonance assignment of protein 1 H‐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 15 N atom. By this means, ambiguities arising from chemical shift degeneracy of amide proton resonances can be resolved. The experiments described involve combining the 1 H‐detected heteronuclear multiple quantum coherence correlation experiment with homonuclear nuclear Overhauser enhancement, J ‐correlated or Hartmann‐Hahn experiments.