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Inside Back Cover: Significant Expansion of the Fluorescent Protein Chromophore through the Genetic Incorporation of a Metal‐Chelating Unnatural Amino Acid (Angew. Chem. Int. Ed. 18/2013)
Author(s) -
Liu Xiaohong,
Li Jiasong,
Hu Cheng,
Zhou Qing,
Zhang Wei,
Hu Meirong,
Zhou Juanzuo,
Wang Jiangyun
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201302113
Subject(s) - fluorescence , chromophore , chelation , amino acid , chemistry , metal , paramagnetism , fluorescent protein , metalloprotein , photochemistry , green fluorescent protein , biochemistry , organic chemistry , physics , quantum mechanics , gene
A metal‐chelating unnatural amino acid (UAA) with an 8‐hydroxyquinoline functional group (HqAla) was enzymatically synthesized in one step. In their Communication on page 4805 ff., J. Y. Wang and co‐workers show that incorporation of HqAla into fluorescent proteins shifts their emission maxima toward higher wavelengths (red‐shifted). This UAA could be applied to engineering metalloproteins and brighter fluorescent proteins, as well as paramagnetic protein NMR spectroscopy.