Unnatural Amino Acid Mutagenesis of Fluorescent Proteins

Authors

  • Dr. Feng Wang,

    1. Department of Chemistry, The Skaggs Institute for Chemical Biology, 10550 North Torrey Pines Road, La Jolla, CA 92037 (USA)
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  • Dr. Wei Niu,

    1. Department of Chemistry, University of Nebraska – Lincoln, Lincoln, NE 68588 (USA)
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  • Prof. Jiantao Guo,

    Corresponding author
    1. Department of Chemistry, University of Nebraska – Lincoln, Lincoln, NE 68588 (USA)
    • Department of Chemistry, University of Nebraska – Lincoln, Lincoln, NE 68588 (USA)
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  • Prof. Peter G. Schultz

    Corresponding author
    1. Department of Chemistry, The Skaggs Institute for Chemical Biology, 10550 North Torrey Pines Road, La Jolla, CA 92037 (USA)
    • Department of Chemistry, The Skaggs Institute for Chemical Biology, 10550 North Torrey Pines Road, La Jolla, CA 92037 (USA)
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  • This work is supported by grant DE-FG03-00ER46051 from The Division of Materials Sciences, DOE (P.G.S.), the Skaggs Institute for Chemical Biology (P.G.S.), and the New Faculty Startup Fund to J.G. from the Chemistry Department of University of Nebraska – Lincoln.

Abstract

original image

Tyrosin 66 eines grünfluoreszierenden Proteins (GFP) wurde durch nichtnatürliche Aminosäuren, die Boronat-, Azid-, Nitro- und Ketogruppen tragen, ersetzt. Allgemein ist equation image dieser GFP-Mutanten verglichen mit equation image von GFP blauverschoben, und die Fluoreszenzintensität der Boronat-Variante nimmt nach Oxidation zu (siehe Schema). Mit den Röntgenkristallstrukturen der Keto- und Boronat-GFP-Mutanten können ihre veränderten Fluoreszenzeigenschaften erklärt werden.

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