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. 2021 Dec 21;44(1):1–13. doi: 10.3390/cimb44010001

Figure 1.

Figure 1

(a) C-15867 ribbon model: the N-ter loop, the α-helix region and the C-ter β-sheet are shown in different colors; (b) hydrophobicity surface of the C-15867 peptide. Hydrophobic residues are in orange-red while hydrophilic residues are highlighted in blue. The figure was generated with UCSF CHIMERA software [45]; (c) Cys3, Cys15, Cys19, Cys30, Cys36, Cys38 residues present in C-15867 peptide; (d) disulfide bonds pattern of C15867 predicted through the DISULFIND server. The figure was generated with UCSF CHIMERA software [45].