Journal of Biomolecular NMR

, Volume 39, Issue 4, pp 275–289

Combined chemical shift changes and amino acid specific chemical shift mapping of protein–protein interactions

  • Frank H. Schumann
  • Hubert Riepl
  • Till Maurer
  • Wolfram Gronwald
  • Klaus-Peter Neidig
  • Hans Robert Kalbitzer
Article

DOI: 10.1007/s10858-007-9197-z

Cite this article as:
Schumann, F.H., Riepl, H., Maurer, T. et al. J Biomol NMR (2007) 39: 275. doi:10.1007/s10858-007-9197-z

Abstract

Protein–protein interactions are often studied by chemical shift mapping using solution NMR spectroscopy. When heteronuclear data are available the interaction interface is usually predicted by combining the chemical shift changes of different nuclei to a single quantity, the combined chemical shift perturbation \(\Updelta \delta_{\rm comb}.\) In this paper different procedures (published and non-published) to calculate \(\Updelta \delta_{\rm comb}\) are examined that include a variety of different functional forms and weighting factors for each nucleus. The predictive power of all shift mapping methods depends on the magnitude of the overlap of the chemical shift distributions of interacting and non-interacting residues and the cut-off criterion used. In general, the quality of the prediction on the basis of chemical shift changes alone is rather unsatisfactory but the combination of chemical shift changes on the basis of the Hamming or the Euclidian distance can improve the result. The corrected standard deviation to zero of the combined chemical shift changes can provide a reasonable cut-off criterion. As we show combined chemical shifts can also be applied for a more reliable quantitative evaluation of titration data.

Keywords

Chemical shift mappingCombined chemical shiftNMRProtein–protein interaction

Copyright information

© Springer Science+Business Media B.V. 2007

Authors and Affiliations

  • Frank H. Schumann
    • 1
  • Hubert Riepl
    • 1
  • Till Maurer
    • 2
  • Wolfram Gronwald
    • 1
  • Klaus-Peter Neidig
    • 3
  • Hans Robert Kalbitzer
    • 1
  1. 1.Institute of Biophysics and Physical BiochemistryUniversity of RegensburgRegensburgGermany
  2. 2.Analytical Sciences DepartmentBoehringer Ingelheim Pharma GmbH & Co. KGIngelheim am RheinGermany
  3. 3.Software DepartmentBruker BioSpin GmbHRheinstettenGermany