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Updated: Mar 20, 2026

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
Published on: July 25, 2013
13-Helix folding of a β/γ-peptide manifold designed from a "minimal-constraint" blueprint
Claire M Grison1, Sylvie Robin2, David J Aitken1
1CP3A Organic Synthesis Group, ICMMO, UMR 8182, CNRS, Université Paris-Sud, Université Paris-Saclay, 15 Rue Georges Clemenceau, 91405 Orsay cedex, France. david.aitken@u-psud.fr.
Abstract:
A bottom-up design rationale was adopted to devise β/γ-peptide foldamer manifolds which would adopt preferred 13-helix conformations, relying on minimal steric imposition brought by the constituent amino acid residues. In this way, a well-defined 13-helix conformer was revealed for short oligomers of trans-2-aminocyclobutanecarboxylic acid and γ(4)-amino acids in alternation, which gave good topological superposition upon an α-helix motif.
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