Figure 2 | Scientific Reports

Figure 2

From: Temporin L and aurein 2.5 have identical conformations but subtly distinct membrane and antibacterial activities

Figure 2

Secondary structure analysis of aurein 2.5 and temporin L peptides from MD simulations. Mean dihedral angles (psi) (upper plot) and their circular variance (lower plot) are shown for each residue to enable identification of regiospecific changes in conformation and/or flexibility. Angles were averaged over 100 ns of simulation and eight aurein 2.5 (A,B) or temporin L (C,D) peptides when binding to POPE/POPG (A,C) or POPG (B,D) membranes. Backbone dihedral angles (psi) for residues in α-helix conformation are around −45°.

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