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  Design of protein congeners containing β-cyclopropylalanine

Acevedo-Rocha, C. G., Geiermann, A.-S., Budisa, N., & Avci, M. (2012). Design of protein congeners containing β-cyclopropylalanine. Molecular BioSystems, 8(10), 2719-2723. doi:10.1039/c2mb25193k.

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 Creators:
Acevedo-Rocha, Carlos G.1, 2, Author              
Geiermann, Anna-S.3, Author
Budisa, Nediljko4, Author
Avci, M.1, Author              
Affiliations:
1Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society, Kaiser-Wilhelm-Platz 1, 45470 Mülheim an der Ruhr, DE, ou_1445588              
2Philipps-Universita¨t Marburg, Fachbereich Chemie,, ou_persistent22              
3Leopold Franzens University, Institute of Organic Chemistry,, ou_persistent22              
4Berlin Institute of Technology, Department of Chemistry,, ou_persistent22              

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 Abstract: The non-canonical amino acid (ncAA) analogue of methionine (Met), b-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.

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 Dates: 2012-10
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: DOI: 10.1039/c2mb25193k
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Title: Molecular BioSystems
Source Genre: Journal
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Pages: - Volume / Issue: 8 (10) Sequence Number: - Start / End Page: 2719 - 2723 Identifier: -