Journal of Biomolecular NMR

, Volume 55, Issue 4, pp 311–321

BEST-TROSY experiments for time-efficient sequential resonance assignment of large disordered proteins

  • Zsofia Solyom
  • Melanie Schwarten
  • Leonhard Geist
  • Robert Konrat
  • Dieter Willbold
  • Bernhard Brutscher
Article

DOI: 10.1007/s10858-013-9715-0

Cite this article as:
Solyom, Z., Schwarten, M., Geist, L. et al. J Biomol NMR (2013) 55: 311. doi:10.1007/s10858-013-9715-0

Abstract

The characterization of the conformational properties of intrinsically disordered proteins (IDPs), and their interaction modes with physiological partners has recently become a major research topic for understanding biological function on the molecular level. Although multidimensional NMR spectroscopy is the technique of choice for the study of IDPs at atomic resolution, the intrinsically low resolution, and the large peak intensity variations often observed in NMR spectra of IDPs call for resolution- and sensitivity-optimized pulse schemes. We present here a set of amide proton-detected 3D BEST-TROSY correlation experiments that yield the required sensitivity and spectral resolution for time-efficient sequential resonance assignment of large IDPs. In addition, we introduce two proline-edited 2D experiments that allow unambiguous identification of residues adjacent to proline that is one of the most abundant amino acids in IDPs. The performance of these experiments, and the advantages of BEST-TROSY pulse schemes are discussed and illustrated for two IDPs of similar length (~270 residues) but with different conformational sampling properties.

Keywords

BEST TROSY IDP Viral protein Amino-acid-type editing Longitudinal-relaxation enhancement 

Supplementary material

10858_2013_9715_MOESM1_ESM.docx (396 kb)
Supplementary material 1 (DOCX 396 kb)

Copyright information

© Springer Science+Business Media Dordrecht 2013

Authors and Affiliations

  • Zsofia Solyom
    • 1
    • 2
    • 3
  • Melanie Schwarten
    • 1
    • 2
    • 3
  • Leonhard Geist
    • 6
  • Robert Konrat
    • 6
  • Dieter Willbold
    • 2
    • 4
    • 5
  • Bernhard Brutscher
    • 1
    • 2
    • 3
  1. 1.Institut de Biologie StructuraleUniversité Grenoble 1Grenoble Cedex 1France
  2. 2.Commissariat à l’Energie Atomique et aux Energies Alternatives (CEA)GrenobleFrance
  3. 3.Centre National de Recherche Scientifique (CNRS)GrenobleFrance
  4. 4.Institute of Complex Systems (ICS-6) Structural Biochemistry, Forschungszentrum JülichJülichGermany
  5. 5.Institut für Physikalische BiologieHeinrich-Heine-UniversitätDüsseldorfGermany
  6. 6.Department of Computational and Structural BiologyMax F. Perutz LaboratoriesViennaAustria

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