Figure 1
From: Tuneable poration: host defense peptides as sequence probes for antimicrobial mechanisms
Cecropin sequence probes. Peptide sequences, linear (a) and configured on helical wheels (b). Blue and grey cylinders denote helical N-terminal (blue) and C-terminal (grey) domains. Lysines are in blue, arginines and neutral polar residues are in light blue, relative identities of hydrophobic residues are in yellow. Glycine residues are in red and glycine zippers are highlighted by overarching horizontal brown brackets. Glycine residues in ChoC and their replacements in ChoM are in orange in the helical wheels. Green lines in the helical wheels of ChoC and ChoM indicate polar angles. The AGPA hinge and the W2 residue are underlined. A coiled-coil designation, gabcdef, is shown along the CecM sequence. Heptad repeats are shown underneath. Only two i, i + 7 pairs are given for clarity. (c) A schematic representation of a carpet-like mechanism by CecB oriented flat on a phospholipid bilayer. For clarity, only one phospholipid per leaflet is shown (aliphatic chains in grey, headgroups in pink).
