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

Abstract
A method is described for sequential resonance assignment of protein 1H‐NMR spectra relying on the detection of long‐range correlations between 15N and CαH atoms using 1H‐detected heteronuclear multiple‐bond correlation spectroscopy. In particular, the observation of the two‐bond 15N(i)‐CαH(i) and three‐bond 15N(i)‐CαH(i−1) correlations enables one to connect one residue with the next. Because the magnitude of the long‐range couplings is small (15N‐enriched protein samples. Further, because the size of the 15N(i)‐CαH(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.

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