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. 2017 Aug 17;2(8):4621–4631. doi: 10.1021/acsomega.7b00639

Figure 2.

Figure 2

Structural comparison of the wild-type α-conotoxins Vc1.1, BuIA, ImI, and AuIB and their disulfide-deleted analogues from 100 ns MD simulations. (A,D,G,J) rmsd for backbone Cα of the wild-type (black line) and mutant (red line) conotoxins. (B,C,E,F,H,I,K,L) Backbone conformation of the peptides extracted from the last 50 ns MD trajectories with equal time intervals. ▼ indicates the time phase when rmsd significantly fluctuated. Values of the Hα chemical shift deviation from the wild-type peptide are used to evaluate the mutational effect on the peptide secondary structure.