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Issue 2, 2000
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Chemical aspects of peptide bond isomerisation

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Abstract

Coplanarity of peptide bonds confers partitioning of peptide chains between two energetically preferred rotational states, cis and trans. Molecular heterogeneity is particularly pronounced when imino acids like proline form the peptide bond. These conformational substates are prone to isomer-specific biochemical recognition, delayed chain folding and biocatalysis of conformational interconversion attracting broad interest in medicinal chemistry and biotechnology. The present review discusses the structural features of peptide bond conformation in oligopeptides and proteins, and gives an overview of isomer ratios, interconversion rates, and catalysis.

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Publication details

The article was received on 31 Aug 1999 and first published on 06 Mar 2000


Article type: Review Article
DOI: 10.1039/A803742F
Citation: Chem. Soc. Rev., 2000,29, 119-127
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    Chemical aspects of peptide bond isomerisation

    G. Fischer, Chem. Soc. Rev., 2000, 29, 119
    DOI: 10.1039/A803742F

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