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Published May 22, 2002 | Version Supplemental Material + Published
Journal Article Open

A designed phenylalanyl-tRNA synthetase variant allows efficient in vivo incorporation of aryl ketone functionality into proteins

Creators

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

Identifiers

Eprint ID
24112
Resolver ID
CaltechAUTHORS:20110620-160431532

Funding

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

Dates

Created
2011-09-27
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Updated
2021-11-09
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