Residue-Specialized Membrane Poration Kinetics of Melittin and Its Variants: Insight from Mechanistic Landscapes *

Zhi-Xiong Deng,Jing-Liang Li,Bing Yuan,Kai Yang

Fig. 1 (Color online) Structural demonstration of melittin and three representative gain-of-function variants, MelP1, MelP3 and MelP5. (a) Amino acid sequences of the peptides. Different types of residues are colored differently: grey for hydrophobic residues, orange for hydrophilic ones, while blue for charged ones. Residues in red are the mutated ones from parent melittin. Arrow "$N$" or "$C$" indicates the $N$ or $C$ terminus of the peptide. (b) Conformational structure of melittin and MelP5 (when binding on a membrane). The two $\alpha$-helixes of melittin are sketched with transparent cylinders, being connected with the kink part between them. Corresponding amino acid residues are highlighted with the same color scheme as in (a).