Journal of Biomolecular NMR

, Volume 31, Issue 2, pp 115–128 | Cite as

A modified strategy for sequence specific assignment of protein NMR spectra based on amino acid type selective experiments

  • Mario Schubert
  • Dirk Labudde
  • Dietmar Leitner
  • Hartmut Oschkinat
  • Peter Schmieder


The determination of the three-dimensional structure of a protein or the study of protein–ligand interactions requires the assignment of all relevant nuclei as an initial step. This is nowadays almost exclusively performed using triple-resonance experiments. The conventional strategy utilizes one or more pairs of three dimensional spectra to obtain redundant information and thus reliable assignments. Here, a modified strategy for obtaining sequence specific assignments based on two dimensional amino acid type selective triple-resonance experiments is proposed. These experiments can be recorded with good resolution in a relatively short time. They provide very specific and redundant information, in particular on sequential connectivities, that drastically increases the ease and reliability of the assignment procedure, done either manually or in an automated fashion. The new strategy is demonstrated with the protein domain PB1 from yeast CDC24p.


amino acid type selective HSQC backbone assignment OPCA motif PB1 domain sequence specific assignment triple-resonance experiments 


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Copyright information

© Springer 2005

Authors and Affiliations

  • Mario Schubert
    • 1
    • 3
  • Dirk Labudde
    • 1
  • Dietmar Leitner
    • 1
  • Hartmut Oschkinat
    • 1
    • 2
  • Peter Schmieder
    • 1
  1. 1.Forschungsinstitut für Molekulare PharmakologieBerlinGermany
  2. 2.Freie Universität BerlinBerlinGermany
  3. 3.Laboratorium für Physikalische ChemieZürichSwitzerland

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