Site-specific incorporation of fluorotyrosines into proteins in Escherichia coli by photochemical disguise.

@article{Wilkins2010SitespecificIO,
  title={Site-specific incorporation of fluorotyrosines into proteins in Escherichia coli by photochemical disguise.},
  author={Bryan Jason Wilkins and Samuel T. Marionni and Douglas D Young and Jia Liu and Yan Wang and Martino Luigi di Salvo and Alexander Deiters and T. Ashton Cropp},
  journal={Biochemistry},
  year={2010},
  volume={49 8},
  pages={1557-9}
}
Fluorinated analogues of tyrosine can be used to manipulate the electronic environments of protein active sites. The ability to selectively mutate tyrosine residues to fluorotyrosines is limited, however, and can currently only be achieved through the total synthesis of proteins. As a general solution to this problem, we genetically encoded the unnatural amino acids o-nitrobenzyl-2-fluorotyrosine, -3-fluorotyrosine, and -2,6-difluorotyrosine in Escherichia coli. These amino acids are disguised… CONTINUE READING

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Fluorescence analysis of sfGFP containing unnatural amino acids 5-8

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