Figure 5
Comparison of amino acid sequence and structural characteristics of helical cathelicidins. Amino acid sequences are shown in the first row of each peptide. The predicted secondary structure (H: helix, S: strand, and C: coil) and solvent accessibility (values range from 0 (buried) to 8 (highly exposed residues)) for the individual residues are shown in the second and third rows of each peptide, respectively. The chemical properties corresponding to each amino acid are indicated in the fourth row of each peptide by different colors, as indicated in parentheses in the following description. “N” and “P” letters indicated nonpolar and polar, respectively. Nonpolar residues contain tryptophan (yellow), phenylalanine (yellow), and aliphatic amino acids (red), while polar residues include uncharged polar (green), positively (blue), and negatively (purple) charged residues and tyrosine (yellow). The unique motif, “N(n≥3)-P(n≥1)-N(n≥3)” was highlighted in grey.