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Published February 15, 2008 | Version Supplemental Material
Journal Article Open

Enzymatic N-terminal Addition of Noncanonical Amino Acids to Peptides and Proteins

Creators

  • 1. ROR icon California Institute of Technology

Abstract

A chromatographic assay was used to identify ten noncanonical amino acids that can be appended to the N terminus of peptides and proteins by the L,F-transferase of Escherichia coli. A model protein substrate, E. coli dihydrofolate reductase, was modified with p-ethynylphenylalanine and conjugated to azide–biotin and azide–polyethylene glycol–fluorescein probes (see scheme).

Additional Information

© 2008 WILEY-VCH Verlag GmbH & Co. Received: October 10, 2007. Published online on January 18, 2008. This work was supported by NIH grant GM62523 (to D.A.T.), NIH grant DK39520 (to A.V.), the ARO-sponsored Institute for Collaborative Biotechnologies, and the Beckman Institute at Caltech. We thank Christina Smolke for use of the Molecular Imager and Mona Shahgholi for help with mass spectrometry. Pin Wang and A. James Link kindly provided the purified synthetases. Edman degradation was performed by the Peptide and Protein Molecular Analysis Laboratory of the Beckman Institute at Caltech.

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Additional details

Identifiers

Eprint ID
53576
DOI
10.1002/cbic.200700605
Resolver ID
CaltechAUTHORS:20150112-114337627

Related works

Describes
10.1002/cbic.200700605 (DOI)

Funding

NIH
GM62523
NIH
DK39520
Army Research Office (ARO)
Caltech Beckman Institute

Dates

Created
2015-01-12
Created from EPrint's datestamp field
Updated
2021-11-10
Created from EPrint's last_modified field