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Long‐range 15 N‐ 1 H correlation as an aid to sequential proton resonance assignment of proteins Application to the DNA‐binding protein ner from phage Mu
Author(s) -
Clore G.Marius,
Bax Ad,
Wingfield Paul,
Gronenborn Angela M.
Publication year - 1988
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(88)80216-3
Subject(s) - heteronuclear molecule , chemistry , proton , crystallography , nuclear magnetic resonance spectroscopy , spectroscopy , resonance (particle physics) , two dimensional nuclear magnetic resonance spectroscopy , stereochemistry , analytical chemistry (journal) , physics , atomic physics , nuclear physics , quantum mechanics , chromatography
A method is described for sequential resonance assignment of protein 1 H‐NMR spectra relying on the detection of long‐range correlations between 15 N and C α H atoms using 1 H‐detected heteronuclear multiple‐bond correlation spectroscopy. In particular, the observation of the two‐bond 15 N( i )‐C α H( i ) and three‐bond 15 N( i )‐C α H( 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 15 N‐enriched protein samples. Further, because the size of the 15 N( i )‐C α H( 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.