Characterizing Changes in the Rate of Protein-Protein Dissociation upon Interface Mutation Using Hotspot Energy and Organization
Figure 9
Stability regions, interface-area and complex-size.
The changes in hotspot energies upon mutation are assessed at three interface regions, which enable us to explore changes in the distribution of stability for complexes of different size and interface-area. CORE, RIM and SUPP represent the PCCs of CoreHSEnergy/RimHSEnergy/SuppHSEnergy averaged for the 6 hotspot prediction algorithms with Δlog10(koff).(A) PCCs for mutants on Complexes with interface-area >1600 Å2 (LIA). (B) PCCs for mutants on complexes with interface-area <1600 Å2 (SIA). (C) PCCs for mutants on complexes with size <500 residues (SCS). (D) PCCs for mutants on complexes with size >500 residues (LCS). (E) LIA-SCS, (F) LIA-LCS, (G) SIA-SCS, (H) SIA-LCS. (I) Scatter plot of complex size vs. interface area for all complexes in off-rate mutant dataset. Here it is observed that complex stability is distributed across all three regions for small-size complexes (C, E and G), whereas the core becomes a localized region of stability for large-complex sizes (D, F, H). On analysis of the interface-area vs. complex-size subsets (E–H), the distribution of stability regions is affected primarily through complex-size irrespective of interface-area.