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Figure 1.
Chemical structures and helical wheel diagrams of 1–9. (A)
Primary sequences of α-peptide 1 and α/β-peptides 2–9,
sorted according to α/β backbone pattern. Bold letters
indicate hydrophobic core residues in the GCN4-pLI sequence.
Colored circles indicate sequence positions occupied by
β-residues, cyan for β^3-residues and orange for cyclic
β-residues. (B) Helical wheel diagram of 1 with hydrophobic
core residues indicated. (C) Structures of an α-amino acid, a
β^3-amino acid, and the cyclic β-amino acids ACPC (X) and APC
(Z). (D) Helical wheel diagrams of the α/β residue patterns of
2–9 based on a heptad repeat. Each circle represents a residue
and is colored by residue type, yellow for α-residues, cyan for
β^3-residues, and orange for cyclic β-residues. Bold circles
indicate hydrophobic core positions.
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