Correlation between 15N NMR chemical shifts in proteins and secondary structure

Hongbiao Le, Eric Oldfield

Research output: Contribution to journalArticlepeer-review


An empirical correlation between the peptide 15N chemical shift, δ15Ni, and the backbone torsion angles φi, ψi-1 is reported. By using two-dimensional shielding surfaces Δ(φiψ1-1), it is possible in many cases to make reasonably accurate predictions of 15N chemical shifts for a given structure. On average, the rms error between experiment and prediction is about 3.5 ppm. Results for threonine, valine and isoleucine are worse (∼4.8 ppm), due presumably to χ1-distribution/γ-gauche effects. The rms errors for the other amino acids are ∼3 ppm, for a typical maximal chemical shift range of ∼15-20 ppm. Thus, there is a significant correlation between 15N chemical shift and secondary structure.

Original languageEnglish (US)
Pages (from-to)341-348
Number of pages8
JournalJournal of Biomolecular NMR
Issue number3
StatePublished - May 1994


  • N shielding
  • Secondary structure
  • Shielding surface
  • Torsion angle

ASJC Scopus subject areas

  • Biochemistry
  • Spectroscopy


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