Interplay between Chaperones and Protein Disorder Promotes the Evolution of Protein Networks
Figure 2
λ describes the evolution of intrinsically disordered proteins.
Proteins are classified according to their percentage of residues that is predicted to be disordered (S: <10%, M: 10–30%, U: >30%). A The evolutionary rate ratio ω is largely independent of the level of protein structuredness for proteins sampled with similar levels of expression. B The evolutionary rate ratio λ increases with increasing protein disorder. C Comparison of the local sequence variability and conservation of the unstructured regions (stretch) to the immediately adjacent structured flanking regions (flank) with the Rate4Site algorithm [41] indicates compensatory selective pressure in the flanking regions. D Protein half-lives on average decrease with increasing protein disorder. Significance levels are indicated as n.s. (not significant), and *** (p<0.001).