ZFIN Image: Nikapitiya et al., 2020, Figure 1

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Figure Caption

Figure 1

Predicted helical secondary and three-dimensional structures of Octominin. (A) Helical wheel of Octominin shows the AAs arrangement and the residue numbers which are counted from the amino (N) terminal of the peptide. The hydrophilic and hydrophobic residues are represented by circles and diamonds, respectively. The potentially charged (positively charged) residues are marked as pentagons in light blue. The most hydrophobic residue is green, and the amount of green is decreasing proportionally to the hydrophobicity, with zero hydrophobicity coded as yellow. (B) Three-dimensional structure and AA sequence of Octominin with positively charged residues.

Acknowledgments

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