Journal of Biomolecular NMR

, Volume 49, Issue 2, pp 139–149

Random coil chemical shift for intrinsically disordered proteins: effects of temperature and pH

  • Magnus Kjaergaard
  • Søren Brander
  • Flemming M. Poulsen
Article

DOI: 10.1007/s10858-011-9472-x

Cite this article as:
Kjaergaard, M., Brander, S. & Poulsen, F.M. J Biomol NMR (2011) 49: 139. doi:10.1007/s10858-011-9472-x

Abstract

Secondary chemical shift analysis is the main NMR method for detection of transiently formed secondary structure in intrinsically disordered proteins. The quality of the secondary chemical shifts is dependent on an appropriate choice of random coil chemical shifts. We report random coil chemical shifts and sequence correction factors determined for a GGXGG peptide series following the approach of Schwarzinger et al. (J Am Chem Soc 123(13):2970–2978, 2001). The chemical shifts are determined at neutral pH in order to match the conditions of most studies of intrinsically disordered proteins. Temperature has a non-negligible effect on the 13C random coil chemical shifts, so temperature coefficients are reported for the random coil chemical shifts to allow extrapolation to other temperatures. The pH dependence of the histidine random coil chemical shifts is investigated in a titration series, which allows the accurate random coil chemical shifts to be obtained at any pH. By correcting the random coil chemical shifts for the effects of temperature and pH, systematic biases of the secondary chemical shifts are minimized, which will improve the reliability of detection of transient secondary structure in disordered proteins.

Keywords

Natively unfolded protein Peptide NMR Protonation state Secondary chemical shift analysis 

Copyright information

© Springer Science+Business Media B.V. 2011

Authors and Affiliations

  • Magnus Kjaergaard
    • 1
  • Søren Brander
    • 1
  • Flemming M. Poulsen
    • 1
  1. 1.Department of BiologyUniversity of CopenhagenKøbenhavn NDenmark