Figure 1 | Scientific Reports

Figure 1

From: Structural flexibility of apolipoprotein E-derived arginine-rich peptides improves their cell penetration capability

Figure 1

Design of stapled A2-17 (StpA2-17) and stitched A2-17 (StchA2-17) peptides. Helical wheel and helical net diagrams of A2-17 are used to display the site where the chemical linkage is introduced to StpA2-17 and StchA2-17. The helical wheel is arranged as an ideal α-helix (100° rotation per residue) as observed from the top of the long axis from the amino-terminal end. The blue and black circles indicate polar and non-polar residues, respectively. The position of red arrow in the helical wheel plot indicates the orientation of the hydrophobic moment of the peptide.

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