Angewandte Chemie International Edition,Article first published online: 28 MAR 2013,DOI: 10.1002/anie.201301307
Significant Expansion of the Fluorescent Protein Chromophore through the Genetic Incorporation of a Metal-Chelating Unnatural Amino Acid
Xiaohong Liu 1,?, Jiasong Li 1,2,?, Cheng Hu1, Qing Zhou1, Wei Zhang 1, Meirong Hu1, Juanzuo Zhou1, Jiangyun Wang1,*
Abstract
A novel metal-chelating unnatural amino acid with an 8-hydroxyquinoline group (HqAla) can be enzymatically incorporated into GFP (see scheme). Substituting a Tyr residue in the chromophore of FPs with HqAla results in significantly red-shifted excitation and emission maxima. The crystal structure of superfolder GFP bearing HqAla in its chromophore shows the structural basis for these red shifts.
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