Figure 1

Distribution of parameters capturing structural change for Control and Test datasets. Distribution of values for the parameters A). Cα RMSD B). %PB changes and C). PB substitution scores calculated at a per-protein level for Control-Rigid, Control-Monomer and PPC datasets. Buried residues are indicated with filled boxes. Ires - interacting residues; NonIres - non-interacting residues; Core_Res (≤5% RSA) - buried residues; Surf10_RSA (>10% RSA) – surface residues. The figure shows that protein-protein complexes undergo significantly larger structural changes when compared with unliganded forms for all residues types. The p-values for all of the following comparisons performed using Mann–Whitney test indicates statistical significance (p-value < 0.0001) : M-All_Res vs. P-All_Res, M-Core_Res vs. P-Core_Res, and M-Surf10_RSA vs. P-Surf10_RSA, for all the 3 parameters. This trend is prominently captured by the parameters Cα RMSD and %PB changes.