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={B. Wilkins and Samuel T. Marionni and D. Young and J. Liu and Y. Wang and M. D. di Salvo and A. Deiters and T. 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… Expand

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