Quantitative prediction of ensemble dynamics, shapes and contact propensities of intrinsically disordered proteins
Fig 5
Number of close contacts formed by each residue during MD simulations of p53TAD and Pup (without outliers) along with average residue-type specific contact propensities.
For each residue, the number of contacts was normalized by the number of snapshots for (A) p53TAD and (B) Pup. Residues with their number of contacts per snapshot below 0.5 are depicted in blue, 0.5–1.5 in black, 1.5–2 in yellow, and above 2 in red. Primary sequences of p53TAD and Pup are given at the bottom and colored as in Panels A, B. Average contact propensities according to amino-acid residue type, which is the number of contacts per snapshot averaged over all residues of the same type, are shown for (C) p53TAD and (D) Pup. Error bars correspond to the standard deviations among different residues of the same type.