Protein α-Turns Recreated in Structurally Stable Small Molecules

Authors

  • Dr. Huy N. Hoang,

    1. Division of Chemistry and Structural Biology, Institute for Molecular Bioscience, The University of Queensland, Brisbane, Qld 4072 (Australia)
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  • Dr. Russell W. Driver,

    1. Division of Chemistry and Structural Biology, Institute for Molecular Bioscience, The University of Queensland, Brisbane, Qld 4072 (Australia)
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  • Dr. Renée L. Beyer,

    1. Division of Chemistry and Structural Biology, Institute for Molecular Bioscience, The University of Queensland, Brisbane, Qld 4072 (Australia)
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  • Dr. Alpeshkumar K. Malde,

    1. School of Chemistry and Molecular Biosciences (SCMB), The University of Queensland, Brisbane, Qld 4072 (Australia)
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  • Dr. Giang T. Le,

    1. Division of Chemistry and Structural Biology, Institute for Molecular Bioscience, The University of Queensland, Brisbane, Qld 4072 (Australia)
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  • Dr. Giovanni Abbenante,

    1. Division of Chemistry and Structural Biology, Institute for Molecular Bioscience, The University of Queensland, Brisbane, Qld 4072 (Australia)
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  • Prof. Alan E. Mark,

    1. Division of Chemistry and Structural Biology, Institute for Molecular Bioscience, The University of Queensland, Brisbane, Qld 4072 (Australia)
    2. School of Chemistry and Molecular Biosciences (SCMB), The University of Queensland, Brisbane, Qld 4072 (Australia)
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  • Prof. David P. Fairlie

    Corresponding author
    1. Division of Chemistry and Structural Biology, Institute for Molecular Bioscience, The University of Queensland, Brisbane, Qld 4072 (Australia)
    • Division of Chemistry and Structural Biology, Institute for Molecular Bioscience, The University of Queensland, Brisbane, Qld 4072 (Australia)
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  • We thank the Australian Research Council for research support and for a Federation Fellowship to D.P.F. (FF0668733 and DP1096290).

Abstract

original image

Kleine Nachahmer: α-Windungen in Proteinen variieren in drei Sätzen von (ϕ,ψ)-Winkeln, die die Form des Peptidrückgrats und die Ganghöhe der Helix bestimmen. Für die cyclischen Tetrapeptide 1 und 2 wird gezeigt, dass sie die Strukturen zweier wichtiger Arten von α-Windungen wiedergeben, die in Schlüsselpositionen von 20 untersuchten Proteinen vorkommen. NMR- und CD-spektroskopische Daten sowie Moleküldynamiksimulationen charakterisieren diese ersten Beispiele nichthelicaler α-Windungen in kleinen Molekülen.

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