Journal of Biomolecular NMR

, Volume 22, Issue 4, pp 349–363

Automated NMR determination of protein backbone dihedral angles from cross-correlated spin relaxation

Article

DOI: 10.1023/A:1014936319712

Cite this article as:
Kloiber, K., Schüler, W. & Konrat, R. J Biomol NMR (2002) 22: 349. doi:10.1023/A:1014936319712
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Abstract

The simultaneous interpretation of a suite of dipole-dipole and dipole-CSA cross-correlation rates involving the backbone nuclei 13Cα, 1Hα,13CO, 15N and 1HN can be used to resolve the ambiguities associated with each individual cross-correlation rate. The method is based on the transformation of experimental cross-correlation rates via calculated values based on standard peptide plane geometry and solid-state 13CO CSA parameters into a dihedral angle probability surface. Triple resonance NMR experiments with improved sensitivity have been devised for the quantification of relaxation interference between 1Hα(i)-13Cα(i)/15N(i)-1HN(i) and 1Hα(i−1)-13Cα(i−1)/15N(i)-1HN(i) dipole-dipole mechanisms in 15N,13C-labeled proteins. The approach is illustrated with an application to 13C,15N-labeled ubiquitin.

chemical shift anisotropycross-correlated spin relaxationdihedral anglesmultiple-quantum coherenceNMR spectroscopyprotein structure determination

Copyright information

© Kluwer Academic Publishers 2002

Authors and Affiliations

  • Karin Kloiber
    • 1
  • Wolfgang Schüler
    • 2
  • Robert Konrat
    • 3
  1. 1.Protein Engineering Network Centers of Excellence and Department of Medical Genetics and Microbiology, Biochemistry and ChemistryUniversity of TorontoTorontoCanada
  2. 2.ProCeryon Biosciences GmbHSalzburgAustria
  3. 3.Institute of Theoretical Chemistry and Molecular Structural BiologyUniversity of ViennaAustria