Published May 22, 2002
| Supplemental Material + Published
Journal Article
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A designed phenylalanyl-tRNA synthetase variant allows efficient in vivo incorporation of aryl ketone functionality into proteins
Abstract
Incorporation of non-natural amino acids into proteins in vivo expands the scope of protein synthesis and design. p-Acetylphenylalanine was incorporated into recombinant dihydrofolate reductase (DHFR) in Escherichia coli via a computationally designed mutant form of the phenylalanyl-tRNA synthetase of the host. DHFR outfitted with ketone functionality can be chemoselectively ligated with hydrazide reagents under mild conditions.
Additional Information
© 2002 American Chemical Society. Received December 7, 2001. Publication Date (Web): April 26, 2002. The authors thank William A. Goddard III, Nagarajan Vaidehi, Kent Kirshenbaum, and Yi Tang for helpful discussions. This work was supported by NIH Grants R01-GM62523 and T32-GM08501, the NSF Center for the Science and Engineering of Materials at Caltech, the Howard Hughes Medical Institute, the Ralph M. Parsons Foundation, and an IBM shared University Research Grant.Attached Files
Published - Datta_2002_J_Am_Chem_Soc_A_designed_phenylalanyl-tRNA_synthetase_variant.pdf
Supplemental Material - ja0177096_s1.pdf
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Additional details
- Eprint ID
- 24112
- Resolver ID
- CaltechAUTHORS:20110620-160431532
- NIH
- R01-GM62523
- NIH
- T32-GM08501
- NSF Center for the Science and Engineering of Materials at the California Institute of Technology
- Howard Hughes Medical Institute (HHMI)
- Ralph M. Parsons Foundation
- IBM Shared University Research Grant
- Created
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2011-09-27Created from EPrint's datestamp field
- Updated
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2021-11-09Created from EPrint's last_modified field