Journal of Biomolecular NMR

, Volume 60, Issue 4, pp 231–240 | Cite as

A six-dimensional alpha proton detection-based APSY experiment for backbone assignment of intrinsically disordered proteins

  • Xuejun Yao
  • Stefan Becker
  • Markus ZweckstetterEmail author


Sequence specific resonance assignment is the prerequisite for the NMR-based analysis of the conformational ensembles and their underlying dynamics of intrinsically disordered proteins. However, rapid solvent exchange in intrinsically disordered proteins often complicates assignment strategies based on HN-detection. Here we present a six-dimensional alpha proton detection-based automated projection spectroscopy (APSY) experiment for backbone assignment of intrinsically disordered proteins. The 6D HCACONCAH APSY correlates the six different chemical shifts, Hα(i − 1), Cα(i − 1), C′(i − 1), N(i), Cα(i) and Hα(i). Application to two intrinsically disordered proteins, 140-residue α-synuclein and a 352-residue isoform of Tau, demonstrates that the chemical shift information provided by the 6D HCACONCAH APSY allows efficient backbone resonance assignment of intrinsically disordered proteins.


NMR Intrinsically disordered protein Assignment α-Synuclein APSY Solvent exchange 



We thank Eckhard Mandelkow and Jacek Biernat for the htau23 sample. This work was in part supported by the DFG through ZW71/3-2 and ZW71/7-1.

Supplementary material

10858_2014_9872_MOESM1_ESM.pdf (84 kb)
Supplementary material 1 (PDF 83 kb)


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Copyright information

© Springer Science+Business Media Dordrecht 2014

Authors and Affiliations

  • Xuejun Yao
    • 1
  • Stefan Becker
    • 1
  • Markus Zweckstetter
    • 1
    • 2
    • 3
    Email author
  1. 1.Department for NMR-based Structural BiologyMax Planck Institute for Biophysical ChemistryGöttingenGermany
  2. 2.German Center for Neurodegenerative Diseases (DZNE), GöttingenGöttingenGermany
  3. 3.Center for Nanoscale Microscopy and Molecular Physiology of the BrainUniversity Medical Center GöttingenGöttingenGermany

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