Backbone assignment of proteins with known structure using residual dipolar couplings.

  title={Backbone assignment of proteins with known structure using residual dipolar couplings.},
  author={Young-Sang Jung and Markus Zweckstetter},
  journal={Journal of biomolecular NMR},
  volume={30 1},
A prerequisite for NMR studies of protein-ligand interactions or protein dynamics is the assignment of backbone resonances. Here we demonstrate that protein assignment can significantly be enhanced when experimental dipolar couplings (RDCs) are matched to values back-calculated from a known three-dimensional structure. In case of small proteins, the program MARS allows assignment of more than 90% of backbone resonances without the need for sequential connectivity information. For bigger… CONTINUE READING


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