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4D APSY-HBCB(CG)CDHD experiment for automated assignment of aromatic amino acid side chains in proteins

Krähenbühl, Barbara ; Hiller, Sebastian ; Wider, Gerhard

In: Journal of Biomolecular NMR, 2011, vol. 51, no. 3, p. 313-318

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    Titre
    • 4D APSY-HBCB(CG)CDHD experiment for automated assignment of aromatic amino acid side chains in proteins
    Auteur
    • Krähenbühl, Barbara. Institute of Molecular Biology and Biophysics, ETH Zurich, 8093, Zurich, Switzerland
    • Hiller, Sebastian. Biozentrum, University of Basel, 4056, Basel, Switzerland
    • Wider, Gerhard. Institute of Molecular Biology and Biophysics, ETH Zurich, 8093, Zurich, Switzerland
    Type de document
    • Postprint
    Langue
    • Anglais
    Publié dans
    • Journal of Biomolecular NMR, 2011, vol. 51, no. 3, p. 313-318. Springer Netherlands
    Autre version électronique
    Identifiant OAI-PMH
    • oai:doc.rero.ch:310617
    Summary
    A four-dimensional (4D) APSY (automated projection spectroscopy)-HBCB(CG)CDHD experiment is presented. This 4D experiment correlates aromatic with aliphatic carbon and proton resonances from the same amino acid side chain of proteins in aqueous solution. It thus allows unambiguous sequence-specific assignment of aromatic amino acid ring signals based on backbone assignments. Compared to conventional 2D approaches, the inclusion of evolution periods on 1Hβ and 13Cδ efficiently removes overlaps, and provides two additional frequencies for consequent automated or manual matching. The experiment was successfully applied to three proteins with molecular weights from 6 to 13kDa. For the complementation of the assignment of the aromatic resonances, TOCSY- or COSY-based versions of a 4D APSY-HCCHaro sequence are proposed