Multi-state design of flexible proteins predicts sequences optimal for conformational change
Fig 7
Relationship of conformational flexibility and native sequence recovery by sequence profiles.
The x axis is binned into three groups of equal number of data points to show the distribution of native sequence recovery between groups of low, middle, and high values for each metric. A Kendall τβ rank correlation test was performed on each profile to measure the strength of dependence of native sequence recovery on each metric, indicated in each plot along with its associated p-value. (A) Comparison of native sequence recovery dependence on maximum RMSD100 between sequence profiles. (B) Comparison of native sequence recovery dependence on RMSDda between sequence profiles. RMSDda values of each protein were not equally distributed, nor were of similar range. Therefore, a z-score of was used to normalize RMSDda values of each protein to compare dihedral angle deviation scores, shown along the x axis. A similar approach was implemented to normalize contact map deviation scores. (C) Comparison of native sequence recovery dependence on contact deviation scores.