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- W2896384800 abstract "The front cover picture shows the reversible optical switching of protein function through site-specific incorporation of different azobenzene-modified phenylalanines into proteins in cells with an expanded genetic code. The photochemical properties, such as excitation wavelengths and half-life of the cis isomer, of the optical switches were tuned through the introduction of fluorine substituents. High incorporation efficiency of the unnatural amino acids was observed, and light-controlled on/off switching was achieved in human cells. Computational analysis of the protein dynamics enabled potential azobenzene insertion sites to be predicted, thereby reducing the need for trial-and-error experimentation and placing the design process on a rational foundation. More information can be found in the full paper by A. Deiters et al. on page 2178 in Issue 20, 2018 (DOI: 10.1002/cbic.201800226)." @default.
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- W2896384800 date "2018-10-01" @default.
- W2896384800 modified "2023-09-27" @default.
- W2896384800 title "Front Cover: Reversible and Tunable Photoswitching of Protein Function through Genetic Encoding of Azobenzene Amino Acids in Mammalian Cells (ChemBioChem 20/2018)" @default.
- W2896384800 doi "https://doi.org/10.1002/cbic.201800570" @default.
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