Jump to main content
Jump to site search
Access to RSC content Close the message box

Continue to access RSC content when you are not at your institution. Follow our step-by-step guide.

Issue 10, 2012
Previous Article Next Article

Design of protein congeners containing β-cyclopropylalanine

Author affiliations


The non-canonical amino acid (ncAA) analogue of methionine (Met), β-cyclopropylalanine (Cpa), was successfully incorporated into recombinant proteins expressed in Escherichia coli in a residue-specific manner. Proteins substituted in this way are congeners because they derive from the same gene sequence as the parent protein but contain a fraction of ncAAs. We have expressed congeners using parent and mutant gene sequences of various proteins (lipase, annexin A5, enhanced green fluorescent protein, and barstar) and found that Cpa incorporation is highly dependent on the protein sequence composition. These results indicate that the global amino acid composition of proteins might be a crucial parameter that influences the outcome of unnatural translation. In addition, we could also demonstrate that the chemical nature of the second residue could be essential for successful ncAA incorporation.

Graphical abstract: Design of protein congeners containing β-cyclopropylalanine

Back to tab navigation

Supplementary files

Article information

17 May 2012
12 Jul 2012
First published
13 Jul 2012

Mol. BioSyst., 2012,8, 2719-2723
Article type

Design of protein congeners containing β-cyclopropylalanine

C. G. Acevedo-Rocha, A. Geiermann, N. Budisa and L. Merkel, Mol. BioSyst., 2012, 8, 2719
DOI: 10.1039/C2MB25193K

Search articles by author