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Helices and other secondary structures of β- and γ-peptides

Authors

  • Dieter Seebach,

    Corresponding author
    1. Laboratorium für Organische Chemie der Eidgenössischen Technischen Hochschule Zürich, Wolfgang-Pauli-Strasse 10, CH-8093 Zürich, Switzerland
    • Laboratorium für Organische Chemie der Eidgenössischen Technischen Hochschule Zürich, Wolfgang-Pauli-Strasse 10, CH-8093 Zürich, Switzerland
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  • David F. Hook,

    1. Laboratorium für Organische Chemie der Eidgenössischen Technischen Hochschule Zürich, Wolfgang-Pauli-Strasse 10, CH-8093 Zürich, Switzerland
    Current affiliation:
    1. Novartis Pharma AG, Basel, Switzerland
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  • Alice Glättli

    1. Laboratorium für Physikalische Chemie der Eidgenössischen Technischen Hochschule Zürich, Wolfgang-Pauli-Strasse 10, CH-8093 Zürich, Switzerland
    Current affiliation:
    1. BASF Aktiengesellschaft, Ludwigshafen, Germany
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Abstract

The principal secondary structural motifs adopted by peptides assembled from β-amino acid units are discussed: the 14-, 12-, 10-, 12/10-, and 8-helices, as well as the hairpin turn, extended structures, stacks, and sheets. Features that promote a particular folding propensity are outlined and illustrated by structures determined in solution (NMR) and in the solid-state (x-ray). The N–Cβ–Cα–CO dihedral angles from molecular dynamics simulations, which are indicative of a particular secondary structure, are presented. A brief description of a helix and a turn of γ-peptides is also given. © 2005 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 84: 23–37, 2006

This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

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