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Analysis of Peptide Secondary Structures by Photoactivatable Amino Acid Analogues

Authors

  • Dr. Knut Kölbel,

    Corresponding author
    1. Pharmaceutical Chemistry and Bioanalytics, Martin-Luther-Universität Halle-Wittenberg, Institut für Pharmazie, Wolfgang-Langenbeck-Strasse 4, 06108 Halle (Germany)
    • Pharmaceutical Chemistry and Bioanalytics, Martin-Luther-Universität Halle-Wittenberg, Institut für Pharmazie, Wolfgang-Langenbeck-Strasse 4, 06108 Halle (Germany)
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  • Dr. Christian H. Ihling,

    1. Pharmaceutical Chemistry and Bioanalytics, Martin-Luther-Universität Halle-Wittenberg, Institut für Pharmazie, Wolfgang-Langenbeck-Strasse 4, 06108 Halle (Germany)
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  • Prof. Dr. Andrea Sinz

    Corresponding author
    1. Pharmaceutical Chemistry and Bioanalytics, Martin-Luther-Universität Halle-Wittenberg, Institut für Pharmazie, Wolfgang-Langenbeck-Strasse 4, 06108 Halle (Germany)
    • Pharmaceutical Chemistry and Bioanalytics, Martin-Luther-Universität Halle-Wittenberg, Institut für Pharmazie, Wolfgang-Langenbeck-Strasse 4, 06108 Halle (Germany)
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  • K.K. is funded by the BMBF (ProNet-T3), A.S. acknowledges financial support by the DFG, the EU, and the Land Sachsen-Anhalt.

Abstract

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Photochemical cross-linking was applied to trap intramolecular interactions in peptides. The incorporation of diazirine-labeled amino acid analogues in combination with high-resolution mass spectrometry made it possible to catch reverse-turn conformations within peptides, exactly map their self-interacting surfaces, and discriminate between stable and transient interactions.

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