Automated NMR determination of protein backbone dihedral angles from cross-correlated spin relaxation
- Cite this article as:
- Kloiber, K., Schüler, W. & Konrat, R. J Biomol NMR (2002) 22: 349. doi:10.1023/A:1014936319712
- 72 Downloads
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.