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Keywords:

  • foldamers;
  • helical structures;
  • NMR spectroscopy;
  • α/β-hybrid peptides;
  • β-amino acids
Thumbnail image of graphical abstract

Anti or gauche? trans2,3-Amino acid residues that are known to promote extended structures in their peptides show specific rotamer preferences in response to an intramolecular hydrogen-bonding possibility, which facilitates the 11-helical structures in their 1:1 α,β-hybrid peptides (see figure). Preferences for the gauche conformation for all internal β residues and anti for the C-terminal residue in these peptides were confirmed by NMR spectroscopic and X-ray diffraction experiments.