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Backbone assignment of proteins with known structure using residual dipolar couplings

Journal of Biomolecular NMR volume 30, pages 25–35 (2004)Cite this article

Abstract

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 proteins, we show that the combination of sequential connectivity information with RDC-matching enables more residues to be assigned reliably and backbone assignment to be more robust against missing data. Structural or dynamic deviations from the employed 3D coordinates do not lead to an increased error rate in RDC-supported assignment. RDC-enhanced assignment is particularly useful when chemical shifts and sequential connectivity only provide a few reliable assignments.

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  1. Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, D-37077, Göttingen, Germany

    Young-Sang Jung, Markus Zweckstetter & Markus Zweckstetter

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  1. Young-Sang Jung
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  2. Markus Zweckstetter
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Correspondence to Markus Zweckstetter.

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Jung, YS., Zweckstetter, M. Backbone assignment of proteins with known structure using residual dipolar couplings. J Biomol NMR 30, 25–35 (2004). https://doi.org/10.1023/B:JNMR.0000042955.14647.77

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  • DOI: https://doi.org/10.1023/B:JNMR.0000042955.14647.77

  • assignment
  • maltose-binding protein
  • Mars
  • NMR
  • protein-ligand binding
  • RDC
  • software
  • structural genomics