Figure 1.

Structure and surface representations of the investigated μ-conotoxins. (A) NMR structures of the five μ-conotoxins (GIIIA, KIIIA, PIIIA, SIIIA, and SmIIIA) used in this study represented as a cartoon. The secondary structure elements, α-helix (purple), 3–10 helix (blue), turn (cyan), and coil (white) were generated by STRIDE¹⁹ in visual molecular dynamics (VMD). The cysteine residues forming the disulfide bonds (yellow) were labeled. (B) Molecular surface was generated by SURF²⁰ in VMD, indicating the hydrophobic (white), basic (blue), acidic (red), and hydrophilic (green) regions. All structures were taken from the ConoServer database.^7,21