Fig. 5

Folding landscape of Symmetrin-1 and Symmetrin-3. a The Symmetrin-1 backbone model is shown in white. All residues mutated in Symmetrin-3 are colored. Hydrophobic residues are colored yellow. Hydrophilic residues are colored cyan. b A Cα root mean squared deviation (RMSD) vs. Rosetta energy units/residue plot for a 95-residue α₃β₄ module of Symmetrin-1, representing all designed inter-residue interactions. A funneled folding landscape is apparent. 10,000 ab initio modeling iterations were performed, depicted as green dots. 100 all-atom energy minimizations of the 95-residue fragment were performed, depicted as red dots. c Superposition of the designed 95-residue Symmetrin-1 α₃β₄ module (white) upon the lowest scoring ab initio model (colored by secondary structure). The secondary structural elements and overall topology is preserved. d The Symmetrin-3 backbone model is shown in white. All residues differing from Symmetrin-1 are colored. Hydrophobic residues are colored yellow. Hydrophilic residues are colored cyan. e A Cα root mean squared deviation (RMSD) vs. Rosetta energy units/residue plot for a 95-residue α₃β₄ module of Symmetrin-3, representing all designed inter-residue interactions. A funneled folding landscape is apparent, although funneling is slightly less prominent as compared to Symmetrin-1. 10,000 ab initio modeling iterations were performed, depicted as green dots. 100 all-atom energy minimizations of the 95-residue fragment were performed, depicted as red dots. f Superposition of the designed 95-residue Symmetrin-3 α₃β₄ module (white) upon the lowest scoring ab initio model (colored by secondary structure). The secondary structural elements and overall topology is preserved