Antimicrobial Lactoferrin Peptides: The Hidden Players in the Protective Function of a Multifunctional Protein
Figure 3
Helical wheel representation of (a) magainin 2, (b) bombinin, (c) temporin, (d) lactoferrampin, and (e) cecropin A. The hydrophilic residues are shown as circles, hydrophobic residues as diamonds, potentially negatively charged as triangles, and potentially positively charged as pentagons. Hydrophobicity is color coded as well: the most hydrophobic residue is green, and the amount of green is decreasing proportionally to low hydrophobicity, coded as yellow. Hydrophilic residues are coded red with pure red being the uncharged residues, and the amount of red decreasing proportionally to the hydrophilicity. The potentially charged residues are light blue. (The plots were made using the software created by Don Armstrong and Raphael Zidovetzki. Version: 0.10 p06 12/14/2001 DLA modified by Jim Hu.)
