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Issue 10, 2012
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Design of protein congeners containing β-cyclopropylalanine

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Abstract

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

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Supplementary files

Article information


Submitted
17 May 2012
Accepted
12 Jul 2012
First published
13 Jul 2012

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

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

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