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Journal of Biomolecular NMR

, Volume 37, Issue 3, pp 179–185 | Cite as

Pairwise NMR experiments for the determination of protein backbone dihedral angle Φ based on cross-correlated spin relaxation

  • Hideo TakahashiEmail author
  • Ichio ShimadaEmail author
Original paper

Abstract

Novel cross-correlated spin relaxation (CCR) experiments are described, which measure pairwise CCR rates for obtaining peptide dihedral angles Φ. The experiments utilize intra-HNCA type coherence transfer to refocus 2-bond \({J_{{\rm NC}\alpha}}\) coupling evolution and generate the \({\hbox{N}(i)\hbox{-\!-}\hbox{C}^{\alpha}(i)}\) or \({\hbox{C}^{\prime}(i-1)\hbox{-\!-}\hbox{C}^{\alpha}(i)}\) multiple quantum coherences which are required for measuring the desired CCR rates. The contribution from other coherences is also discussed and an appropriate setting of the evolution delays is presented. These CCR experiments were applied to 15N- and 13C-labeled human ubiquitin. The relevant CCR rates showed a high degree of correlation with the Φ angles observed in the X-ray structure. By utilizing these CCR experiments in combination with those previously established for obtaining dihedral angle Ψ, we can determine high resolution structures of peptides that bind weakly to large target molecules.

Keywords

Chemical shift anisotropy Cross-correlated relaxation Dihedral angle Dipole–dipole interaction Intra-HNCA Structure determination 

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Notes

Acknowledgements

This work was supported by grants from the New Energy and Industrial Technology Development Organization.

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Copyright information

© Springer Science+Business Media B.V. 2007

Authors and Affiliations

  1. 1.Biological Information Research Center (BIRC)National Institute of Advanced Industrial Science and Technology (AIST)TokyoJapan
  2. 2.Graduate School of Pharmaceutical SciencesThe University of TokyoTokyoJapan

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