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. Author manuscript; available in PMC: 2011 Sep 8.
Published in final edited form as: J Am Chem Soc. 2010 Sep 8;132(35):12378–12387. doi: 10.1021/ja103543s

Figure 2.

Figure 2

Ribbon diagrams from x-ray crystal structures of α/β-peptides (A) 5 (PDB: 3HET), (B) 6 (PDB: 3HEU), (C) 7 (PDB: 3HEV), (D) 8 (PDB: 3HEW), (E) 9 (PDB: 3HEX), (F) 10 (PDB: HEY), showing the helix-bundle tetramer quaternary structures formed in each case. α-Amino acid residues are colored yellow, β3-amino acid residues are colored blue, and cyclic β-amino acid residues are colored red. Unlike 2, α/β-peptides 510 have a continuous heptad repeat pattern, without a helical stammer.