Characteristic Structural Parameters for the γ‐Peptide 14‐Helix: Importance of Subunit Preorganization

Abstract

All wound up: Crystallographic data for a set of homologous peptides constructed from gabapentin and two to six preorganized γ-amino acid residues (see crystal structure of the longest peptide) allow derivation of characteristic parameters for the γ-peptide 14-helix and establish guidelines for characterizing 14-helical folding. The results suggest that the substitution pattern of a γ-residue has a profound effect on the propensity for 14-helical folding. Detailed facts of importance to specialist readers are published as ”Supporting Information”. Such documents are peer-reviewed, but not copy-edited or typeset. They are made available as submitted by the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.