Fig. 4: Structural differences between the 100% sequence identical regions of A1 and Sa1.
From: Design and characterization of a protein fold switching network
a Main chain comparisons. (Left panel) CS-Rosetta structure of A1 with color coding for secondary structured elements. (Right panel) Corresponding color-coded regions mapped onto the CS-Rosetta structure of Sa1, illustrating changes in backbone conformation. Regions outside the 56 amino acid sequence of A1 are shown in wheat. b Side chain comparisons. (Left panel) Residues contributing to the core of A1 from the α1-helix (yellow), and from other regions (cyan). The non-α1 core residues from Sa1 (pink) do not overlap with the A1 core (see text for further details). (Right panel) Residues contributing to the core of Sa1 from the α1-helix (yellow), and most of the other participating core residues (pink). The non-α1 core residues from A1 are also shown (cyan), highlighting the low degree of overlap.
