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In vivo incorporation of an alkyne into proteins in Escherichia coli

Academic Article
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Overview

authors

  • Deiters, A.
  • Schultz, Peter

publication date

  • 2005

journal

  • Bioorganic & Medicinal Chemistry Letters  Journal

abstract

  • Using a genetic selection we identified mutants of the M. janaschii tyrosyl-tRNA synthetase that selectively charge an amber suppressor tRNA with para-propargyloxyphenylalanine in Escherichia coli. These evolved tRNA-synthetase pairs were used to site-specifically incorporate an alkynyl group into a protein, which was subsequently conjugated with fluorescent dyes by a [3+2]-cycloaddition reaction under mild reaction conditions.

subject areas

  • Alkynes
  • Animals
  • Cyclization
  • Directed Molecular Evolution
  • Escherichia coli
  • Fluorescent Dyes
  • Molecular Structure
  • Mutation
  • Myoglobin
  • Phenylalanine
  • Protein Engineering
  • Proteins
  • RNA, Transfer
  • Structure-Activity Relationship
  • Tyrosine-tRNA Ligase
  • Whales
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Identity

International Standard Serial Number (ISSN)

  • 0960-894X

Digital Object Identifier (DOI)

  • 10.1016/j.bmcl.2004.12.065

PubMed ID

  • 15713420
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Additional Document Info

start page

  • 1521

end page

  • 1524

volume

  • 15

issue

  • 5

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