Fig. 12. (A) Peptide sequence for CylLL′′. (B) Minimum energy structure of CylLL′′. Residues involved in thioether linkages and dehydroamino acid residues are marked. The helix at the N-terminus has been termed helix A, the helix spanning the hinge region has been termed helix B, while the C-terminal helix has been named helix C. (C) Superimposition of the minimum energy 10 structure ensemble for CylLL′′ with the portion of the peptide corresponding to helix A aligned. Hydrogen bonds are shown in yellow dashed lines.
