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. 2018 Sep 19;6:e5635. doi: 10.7717/peerj.5635

Figure 4. CD spectra of the four peptides (100 µM) in 10 mM ammonium acetate buffer (A) and 50% TFE ammonium acetate buffer (B). Helical wheel projections (Gautier et al., 2008) of peptides (C), with the arrow indicated the direction of the hydrophobic moments.

Figure 4

All the peptides exhibit random coil structure in the aqueous solution while they are able to form α-helical structure in the membrane-mimetic environment. The hydrophobic (yellow), hydrophilic (purple), positively-charged (blue), negatively-charged (red), amide (pink) and small (grey) residues are presented.