Emergence of Protein Fold Families through Rational Design
Figure 2
The Sequence Entropy Computed from Simulations versus the Naturally Occurring Sequence Entropy Computed from HSSP
Three families of protein homologs were studied: HPR domain (A,D,G), ROSSMAN fold (B,E,H), and SH3 domain (C,F,I). The open circles (○) in (A–F) correspond to the functionally important residues. In (G–I), these functionally important residues are shown in stick representation. In (G,H), the SO42− ions are used to mimic the phosphate anion in crystal preparation. In (I), the poly-proline peptide are shown in yellow and the peptide-binding residues form a continuous surface, shown in mesh representation.