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. Author manuscript; available in PMC: 2021 Oct 6.
Published in final edited form as: Structure. 2020 Jun 30;28(10):1114–1123.e4. doi: 10.1016/j.str.2020.04.005

Figure 3. Structural analysis of redesigned cyclic peptides.

Figure 3.

A. Sequence alignment of redesigned peptides compared to the wild-type C05 CDRH3 sequence. Residues with the same identity as wild-type are shown as dashes. The total number of mutations in each peptide is also shown. B-C. Models of redesigned cyclic peptides (tan) are compared to the C05 CDRH3 structure (gray), and Cα RMSD over all residues in the peptide is shown below. The mutations introduced into the peptide sequence in their structural contexts are highlighted.