Journal of Biomolecular NMR

, Volume 22, Issue 4, pp 349-363

First online:

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

  • Karin KloiberAffiliated withProtein Engineering Network Centers of Excellence and Department of Medical Genetics and Microbiology, Biochemistry and Chemistry, University of Toronto
  • , Wolfgang SchülerAffiliated withProCeryon Biosciences GmbH
  • , Robert KonratAffiliated withInstitute of Theoretical Chemistry and Molecular Structural Biology, University of Vienna Email author 

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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 anisotropy cross-correlated spin relaxation dihedral angles multiple-quantum coherence NMR spectroscopy protein structure determination