 Plant antimicrobial peptides, amps, have evolved differently from those found in other life forms. They are rich in cysteine residues, which form multiple disulfides, resulting in exceptional chemical, thermal, and proteolytic stability. These cysteine-rich peptides, also known as cysteine-rich peptides, CRPs, are classified according to their sequence similarity, cysteine motifs, and tertiary structure fold. Thionins, defensins, heathian-like peptides, noden-type peptides, both linear and cyclic, lipid transfer proteins, alphaherpinin, and snake-ins are all examples of CRPs. Additionally, there are amps that are rich in other amino acids. The ability of these peptides to organize into specific families with conserved structural folds enables sequence variation of noncysteine residues to be accommodated within the same scaffold. This allows for diverse functions to be performed by varying the sequence of the noncysteine residues. Furthermore, the ability of... This article was authored by James P. Tam, Xu Jingwang, Ka-H Wang, and others. We are article.tv. Links in the description below.