Site-Specific Incorporation of a Thioester Containing Amino Acid into Proteins | Zendy

Weimin Xuan | Zendy; Daniel P. Collins | Zendy; Minseob Koh | Zendy; Sida Shao | Zendy; Anzhi Yao | Zendy; Han Xiao | Zendy; Philip Garner | Zendy; Peter G. Schultz | Zendy

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Site-Specific Incorporation of a Thioester Containing Amino Acid into Proteins

Author(s) -

Weimin Xuan,

Daniel P. Collins,

Minseob Koh,

Sida Shao,

Anzhi Yao,

Han Xiao,

Philip Garner,

Peter G. Schultz

Publication year - 2018

Publication title -

acs chemical biology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.899

H-Index - 111

eISSN - 1554-8937

pISSN - 1554-8929

DOI - 10.1021/acschembio.7b00998

Subject(s) - thioester , native chemical ligation , fluorophore , biochemistry , transfer rna , amino acid , aspartic acid , chemistry , yield (engineering) , biology , fluorescence , chemical synthesis , rna , in vitro , gene , enzyme , physics , materials science , quantum mechanics , metallurgy

Here, we report the site-specific incorporation of a thioester containing noncanonical amino acid (ncAA) into recombinantly expressed proteins. Specifically, we genetically encoded a thioester-activated aspartic acid (ThioD) in bacteria in good yield and with high fidelity using an orthogonal nonsense suppressor tRNA/aminoacyl-tRNA synthetase (aaRS) pair. To demonstrate the utility of ThioD, we used native chemical ligation to label green fluorescent protein with a fluorophore in good yield.

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