Journal of Biomolecular NMR

, Volume 57, Issue 4, pp 353–361 | Cite as

High-dimensionality 13C direct-detected NMR experiments for the automatic assignment of intrinsically disordered proteins

  • Wolfgang Bermel
  • Isabella C. Felli
  • Leonardo Gonnelli
  • Wiktor Koźmiński
  • Alessandro Piai
  • Roberta Pierattelli
  • Anna Zawadzka-Kazimierczuk
Article

Abstract

We present three novel exclusively heteronuclear 5D 13C direct-detected NMR experiments, namely (HN-flipN)CONCACON, (HCA)CONCACON and (H)CACON(CA)CON, designed for easy sequence-specific resonance assignment of intrinsically disordered proteins (IDPs). The experiments proposed have been optimized to overcome the drawbacks which may dramatically complicate the characterization of IDPs by NMR, namely the small dispersion of chemical shifts and the fast exchange of the amide protons with the solvent. A fast and reliable automatic assignment of α-synuclein chemical shifts was obtained with the Tool for SMFT-based Assignment of Resonances (TSAR) program based on the information provided by these experiments.

Keywords

Intrinsically disordered proteins 13C direct-detection NMR Non-uniform sampling Longitudinal relaxation enhancement Multidimensional NMR experiment Automatic assignment 

Supplementary material

10858_2013_9793_MOESM1_ESM.pdf (2 mb)
Supplementary material 1 (PDF 2000 kb)

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Copyright information

© Springer Science+Business Media Dordrecht 2013

Authors and Affiliations

  • Wolfgang Bermel
    • 1
  • Isabella C. Felli
    • 2
    • 3
  • Leonardo Gonnelli
    • 2
  • Wiktor Koźmiński
    • 4
  • Alessandro Piai
    • 2
  • Roberta Pierattelli
    • 2
    • 3
  • Anna Zawadzka-Kazimierczuk
    • 4
  1. 1.Bruker BioSpin GmbH, SilberstreifenRheinstettenGermany
  2. 2.CERMUniversity of FlorenceSesto FiorentinoItaly
  3. 3.Department of Chemistry “Ugo Schiff”University of FlorenceSesto FiorentinoItaly
  4. 4.Faculty of Chemistry, Biological and Chemical Research CentreUniversity of WarsawWarsawPoland

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