Titelbild: Chemically Programmed Supramolecular Assembly of Hemoprotein and Streptavidin with Alternating Alignment (Angew. Chem. 16/2012)

Authors

  • Dr. Koji Oohora,

    1. Department of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita 565-0871 (Japan)
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  • Sabina Burazerovic,

    1. Department of Chemistry, University of Basel, Spitalstrasse 51, 4056 Basel (Switzerland)
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  • Dr. Akira Onoda,

    1. Department of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita 565-0871 (Japan)
    2. Frontier Research Base for Global Young Researchers, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita 565-0871 (Japan)
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  • Dr. Yvonne M. Wilson,

    1. Department of Chemistry, University of Basel, Spitalstrasse 51, 4056 Basel (Switzerland)
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  • Prof. Dr. Thomas R. Ward,

    Corresponding author
    1. Department of Chemistry, University of Basel, Spitalstrasse 51, 4056 Basel (Switzerland)
    • Department of Chemistry, University of Basel, Spitalstrasse 51, 4056 Basel (Switzerland)
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  • Prof. Dr. Takashi Hayashi

    Corresponding author
    1. Department of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita 565-0871 (Japan)
    • Department of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita 565-0871 (Japan)
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Abstract

original image

Ein alternierendes Proteinassoziat aus dem Myoglobin-Dimer (grün) und Streptavidin (grau) wurde mithilfe einer synthetisierten Cofaktor-Dyade mit einer flexiblen Brücke zwischen einer Hämgruppe (rot) und einer Bis(biotin)-Einheit (blau) erhalten. Die spezifischen Wechselwirkungen zwischen diesen drei Komponenten führten zu einem supramolekularen, submikrometergroßen, faserförmigen Assoziat, das mit AFM analysiert wurde, wie T. Hayashi, T. R. Ward et al. in der Zuschrift auf S. 3884 ff. berichten.

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