<p>This peptide has six cysteines involved in three disulphide bonds.The presence of a 'disulphide through disulphide knot' structurally defines this protein as a knottin: the peptide contains a global fold which involves a cysteine-knotted three-stranded antiparallel beta-sheet along with a flexible loop and four beta-reverse turns. It also has an amphiphilic character which is the main structural basis of its biological function [<cite idref="PUB00013263"/>]. The peptides in this entry belong to the AMP family. </p> Gurmarin/antimicrobial peptide