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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