Multi-state design of flexible proteins predicts sequences optimal for conformational change
Fig 9
Comparison of conformational diversity and per-residue total scores.
All panels are binned into low, medium, and high x values, with equal number of data points for each bin. A Kendall τβ rank correlation test was performed on each profile to measure the strength of dependence of native sequence recovery on the x axis value, indicated in each plot along with its associated p-value. (A) Comparison of maximum RMSD100 and mean total energy score, normalized by the number of residues. (B) Comparison of normalized RMSDda z-score and mean total energy score of each residue. (C) Comparison of normalized contact proximity deviation z-score and mean total energy score of each residue.