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Issue 85, 2016
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Genetically encoded fluorophenylalanines enable insights into the recognition of lysine trimethylation by an epigenetic reader

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Abstract

Fluorophenylalanines bearing 2–5 fluorine atoms at the phenyl ring have been genetically encoded by amber codon. Replacement of F59, a phenylalanine residue that is directly involved in interactions with trimethylated K9 of histone H3, in the Mpp8 chromodomain recombinantly with fluorophenylalanines significantly impairs the binding to a K9-trimethylated H3 peptide.

Graphical abstract: Genetically encoded fluorophenylalanines enable insights into the recognition of lysine trimethylation by an epigenetic reader

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Publication details

The article was received on 20 Jul 2016, accepted on 27 Sep 2016 and first published on 27 Sep 2016


Article type: Communication
DOI: 10.1039/C6CC05959G
Citation: Chem. Commun., 2016,52, 12606-12609
  • Open access: Creative Commons BY license
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    Genetically encoded fluorophenylalanines enable insights into the recognition of lysine trimethylation by an epigenetic reader

    Y. Lee, M. J. Schmidt, J. M. Tharp, A. Weber, A. L. Koenig, H. Zheng, J. Gao, M. L. Waters, D. Summerer and W. R. Liu, Chem. Commun., 2016, 52, 12606
    DOI: 10.1039/C6CC05959G

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