Journal of Biomolecular NMR

, Volume 63, Issue 3, pp 299–307 | Cite as

Improved validation of IDP ensembles by one-bond Cα–Hα scalar couplings

  • Vytautas Gapsys
  • Raghavendran L. Narayanan
  • ShengQi Xiang
  • Bert L. de Groot
  • Markus ZweckstetterEmail author


Intrinsically disordered proteins (IDPs) are best described by ensembles of conformations and a variety of approaches have been developed to determine IDP ensembles. Because of the large number of conformations, however, cross-validation of the determined ensembles by independent experimental data is crucial. The 1JCαHα coupling constant is particularly suited for cross-validation, because it has a large magnitude and mostly depends on the often less accessible dihedral angle ψ. Here, we reinvestigated the connection between 1JCαHα values and protein backbone dihedral angles. We show that accurate amino-acid specific random coil values of the 1JCαHα coupling constant, in combination with a reparameterized empirical Karplus-type equation, allow for reliable cross-validation of molecular ensembles of IDPs.


NMR Intrinsically disordered protein Scalar coupling Ensemble 



We thank Eckhard Mandelkow and Jacek Biernat for the Tau sample. This work was in part supported by the DFG through ZW71/8-1.


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Copyright information

© Springer Science+Business Media Dordrecht 2015

Authors and Affiliations

  • Vytautas Gapsys
    • 1
  • Raghavendran L. Narayanan
    • 2
  • ShengQi Xiang
    • 2
  • Bert L. de Groot
    • 1
  • Markus Zweckstetter
    • 2
    • 3
    • 4
    Email author
  1. 1.Computational Biomolecular Dynamics GroupMax Planck Institute for Biophysical ChemistryGöttingenGermany
  2. 2.Department for NMR-Based Structural BiologyMax Planck Institute for Biophysical ChemistryGöttingenGermany
  3. 3.German Center for Neurodegenerative Diseases (DZNE)GöttingenGermany
  4. 4.Center for Nanoscale Microscopy and Molecular Physiology of the BrainUniversity Medical Center GöttingenGöttingenGermany

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