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Fig. 7. Amino acid sequences of g -core signature motifs among disulfide-containing antimicrobial peptides. Nomenclature and coloration are as indicated in Figs. 2 and 3 of the primary article; standard abbreviations are used for peptide names where appropriate. Lavender shading of molecule identities in Groups IID and IIIB indicates peptides aligned in the levomeric orientation. These sequences correspond to the g -core pattern map as depicted in Figs. 3 and 4 of the primary article.

Fig. 8. Conservation of the multidimensional signature in disulfide-containing antimicrobial peptides. This triple alignment demonstrates the dramatic 3D conservation in antimicrobial peptides from phylogenetically diverse species spanning 2.6 billion years of evolution: fruit fly (Drosophila; 1MYN), mussel (Mytilus; 1FJN), and horse chestnut tree (Aesculus; 1BK8). The striking degree of 3D preservation reflects a unifying structural code among these broad classes of disulfide-containing host defense effector molecules. Alignment was carried out using the Vector Alignment Search Tool (VAST) available through the National Center for Biotechnology Information (NCBI). Secondary structure is indicated by the Cn3D coloration schema: sheet, gold; helix, green; turn/extended, blue. Cn3D can be found through the National Center for Biotechnology Information, a resource of the National Institutes of Health, at www.ncbi.nlm.nih.gov/Structure/CN3D/cn3d.shtml.

Fig. 9. Antimicrobial peptide dataset. The initial antimicrobial peptide dataset used in this analysis was broadly encompassing of antimicrobial peptides from evolutionarily broad host sources, and with diverse sequences and secondary structures of recognized antimicrobial peptide classes. Concatenation indicates the proportionate distribution of peptides representing conventional antimicrobial peptide structure classification and distribution, per the Antimicrobial Sequences Database (www.bbcm.univ.trieste.it/~tossi/pag3.htm) and the Antimicrobial Peptide Database (http://aps.unmc.edu/AP/main.php). Numbers of peptides classified in each group are indicated in brackets for each class. Of the more than 750 peptides present in the database at the onset of the study, the balance of those not indicated comprised peptides representing unusual or other classifications, including macrocyclic, proline-rich, tryptophan-rich or indolicidin-like, and large polypeptides greater than 75 aa in length.