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Article

Discovery of aminoacyl-tRNA synthetase activity through cell-surface display of noncanonical amino acids.

Proceedings of the National Academy of Sciences of the United States of America - 5 Jul 2006

Link A James, Vink Mandy K S, Agard Nicholas J, Prescher Jennifer A, Bertozzi Carolyn R, Tirrell David A

Abstract excerpt

The incorporation of noncanonical amino acids into recombinant proteins in Escherichia coli can be facilitated by the introduction of new aminoacyl-tRNA synthetase activity into the expression host. We describe here a screening procedure for the identification of new aminoacyl-tRNA synthetase activity based on the cell surface display of noncanonical amino acids. Screening of a saturation mutagenesis library of...

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Identifiers

PMID: 16801548
DOI: 10.1073/pnas.0601167103
PMCID: PMC1502431

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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