- Reversible and Tunable Photoswitching of Protein Function through Genetic Encoding of Azobenzene Amino Acids in Mammalian Cells
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The genetic encoding of three different azobenzene phenylalanines with different photochemical properties was achieved in human cells by using an engineered pyrrolysyl tRNA/tRNA synthetase pair. In order to demonstrate reversible light control of protein function, azobenzenes were site-specifically introduced into firefly luciferase. Computational strategies were applied to guide the selection of potential photoswitchable sites that lead to a reversibly controlled luciferase enzyme. In addition, the new azobenzene analogues provide enhanced thermal stability, high photoconversion, and responsiveness to visible light. These small-molecule photoswitches can reversibly photocontrol protein function with excellent spatiotemporal resolution, and preferred sites for incorporation can be computationally determined, thus providing a new tool for investigating biological processes.
- Luo, Ji,Samanta, Subhas,Convertino, Marino,Dokholyan, Nikolay V.,Deiters, Alexander
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- The incorporation of a photoisomerizable amino acid into proteins in E. coli
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An orthogonal aminoacyl tRNA synthetase/tRNA pair has been evolved that allows the incorporation of the photoisomerizable amino acid phenylalanine-4′-azobenzene (AzoPhe) into proteins in E. coli in response to the amber nonsense codon. Further, we show th
- Bose, Mohua,Groff, Dan,Xie, Jianming,Brustad, Eric,Schultz, Peter G.
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- Photoswitching of the Enzymatic Activity of Semisynthetic Ribonuclease S' Bearing Phenylazophenylalanine at a Specific Site
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Photoswitching of the enzymatic activity of ribonuclease S' was successfully carried out by site specific incorporation of phenylazophenylalanine into S-peptide skeleton by semisynthesis.
- Hamachi, Itaru,Hiraoki, Takashi,Yamada, Yasuhiro,Shinkai, Seiji
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p. 704 - 706
(2007/10/03)
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- Photoswitching of the enzymatic activity of semisynthetic ribonuclease S' bearing phenylazophenylalanine at a specific site
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Photos witching of the enzymatic activity of ribonuclease S' was successfully carried out by site specific incorporation of phenylazophenylalanine into S-peptide skeleton by semisynthesis.
- Hamachi, Itaru,Hiraoka, Takashi,Yamada, Yasuhiro,Shinkai, Seiji
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p. 537 - 538
(2007/10/03)
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