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Updated: Jun 21, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
An alpha/beta-peptide helix bundle with a pure beta3-amino acid core and a distinctive quaternary structure
Michael W Giuliano1, W Seth Horne, Samuel H Gellman
1Department of Chemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.
Abstract:
Helix bundles are among the most widely studied tertiary and quaternary structural motifs in proteins. Here we present the crystal structure of an alpha/beta-peptide foldamer that adopts a tetrameric helix-bundle quaternary structure with a hydrophobic core composed solely of beta-amino acids. The structure displays features that are unprecedented among all known helix bundles composed of either alpha-peptides or peptidic foldamers. The tetramer is characterized by an asymmetry of interaction between neighboring helices, and the side-chain packing within the hydrophobic core differs fundamentally from the knobs-into-holes arrangement typical of most helix bundles.
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