Journal of Biomolecular NMR

, Volume 2, Issue 4, pp 401–405 | Cite as

Measurement of two-bond JCOHα coupling constants in proteins uniformly enriched with13C

  • Geerten W. Vuister
  • Ad Bax
Short Communications


A simple E.COSY type technique is described for measurement of two-bond JCOHα coupling constants in proteins that are uniformly enriched with13C. The method has been used to measure2JCOHα for 132 residues in the proteins calmodulin and staphylococcal nuclease having non-overlapping Hα−Cα correlations. Measured2JCOHα coupling constants fall in the 0 to −9.5 Hz range. A separate experiment, measuring the accuracy of these values, indicates a root-mean-square error of 1 Hz. Comparison of the J couplings with the dihedral back bone angles from crystallographic studies confirms a weak but statistically significant correlation between the dihedral angle ψ and the magnitude of2JCOHα, but also indicates that parameters other than ψ have a significant effect on the value of the coupling.


Two-bond J coupling 13C enrichment ψ angle Protein backbone E.COSY 


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Copyright information

© ESCOM Science Publishers B.V 1992

Authors and Affiliations

  • Geerten W. Vuister
    • 1
  • Ad Bax
    • 1
  1. 1.Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney DiseasesNational Institutes of HealthBethesdaUSA

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