Figure 1: Amino acid sequences of α-, β-, and θ-defensins and β-hairpin antimicrobial peptides with their disulfide (SS) bond connectivity with solid lines. | Scientific Reports

Figure 1: Amino acid sequences of α-, β-, and θ-defensins and β-hairpin antimicrobial peptides with their disulfide (SS) bond connectivity with solid lines.

From: Rattusin structure reveals a novel defensin scaffold formed by intermolecular disulfide exchanges

Figure 1

Cysteine, hydrophobic, positively charged, and negatively charged residues are colored with a shade of black, gray, blue, and red shadow, respectively. The amino acid sequence of dimeric rattusin is shown. Cysteine order is indicated in Roman numerals.

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