Zuschrift

Unnatural Amino Acid Mutagenesis of Fluorescent Proteins†

  1. Dr. Feng Wang1,
  2. Dr. Wei Niu2,
  3. Prof. Jiantao Guo2,*,
  4. Prof. Peter G. Schultz1,*

Article first published online: 5 SEP 2012

DOI: 10.1002/ange.201204668

Issue

Angewandte Chemie

Angewandte Chemie

Volume 124, Issue 40, pages 10279–10282, October 1, 2012

Additional Information

How to Cite

Wang, F., Niu, W., Guo, J. and Schultz, P. G. (2012), Unnatural Amino Acid Mutagenesis of Fluorescent Proteins . Angew. Chem., 124: 10279–10282. doi: 10.1002/ange.201204668

Author Information

  1. 1

    Department of Chemistry, The Skaggs Institute for Chemical Biology, 10550 North Torrey Pines Road, La Jolla, CA 92037 (USA)

  2. 2

    Department of Chemistry, University of Nebraska – Lincoln, Lincoln, NE 68588 (USA)

*Department of Chemistry, University of Nebraska – Lincoln, Lincoln, NE 68588 (USA)

  1. †

    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.

Publication History

  1. Issue published online: 26 SEP 2012
  2. Article first published online: 5 SEP 2012
  3. Manuscript Revised: 9 AUG 2012
  4. Manuscript Received: 14 JUN 2012

Funded by

  • Division of Materials Sciences, DOE
  • Skaggs Institute for Chemical Biology
  • Chemistry Department of University of Nebraska – Lincoln

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Keywords:

  • Biosensoren;
  • Fluoreszenz;
  • Fluoreszierende Proteine;
  • Protein-Engineering;
  • Nichtnatürliche Aminosäuren
Thumbnail image of graphical abstract

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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