Expressed protein modifications: Making synthetic proteins

Birgit Wiltschi*

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapter


Techniques to manipulate cellular gene expression such that amino acid analogs not encoded by the genetic code are incorporated into a polypeptide chain have recently gained increasing interest. The so-called noncanonical amino acids often have unusual properties that can be translated into target proteins by reprogrammed ribosomal protein synthesis. Residue-specific substitution of a specific canonical amino acid by its analogs provokes global effects in the resulting protein congeners that include improved stability or catalytic activity, reduced redox sensitivity, as well as altered spectral properties. Thus, the approach holds great promise for the engineering of synthetic proteins. This contribution describes a protocol for the incorporation of a noncanonical amino acid into a target protein expressed in an appropriate amino acid auxotrophic E. coli strain.

Original languageEnglish
Title of host publicationSynthetic Gene Networks
Subtitle of host publicationMethods and Protocols
EditorsWilfried Weber, Martin Fussenegger, Wilfried Weber
Number of pages15
Publication statusPublished - 1 Jan 2012
Externally publishedYes

Publication series

NameMethods in Molecular Biology
ISSN (Print)1064-3745


  • Aminoacyl-tRNA synthetase
  • Auxotrophy
  • Expressed protein modifi cation
  • New minimal medium
  • Noncanonical amino acid
  • Protein engineering
  • Residue-specifi c incorporation
  • Substrate tolerance
  • Unnatural amino acid

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics


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