. 2016 Jun 23;17(Suppl 2):397. doi: 10.1186/s12864-016-2726-y

Table 3.

Relation between thermodynamic properties and structural properties in proteins with biologically functional multimeric assembly

Disease-related variations	RSA ≥ 0.20	RSA < 0.20
\|ΔΔG\| ≤ 1	660 (28.5 %) Monomer^a 465	650 (28.0 %) Monomer^a 24
\|ΔΔG\| ≤ 1	550 (25.0 %) Complex^a 421	760 (31.5 %) Complex^a 68
\|ΔΔG\| > 1	213 (9.2 %) Monomer^a 152	793 (34.2 %) Monomer^a 24
\|ΔΔG\| > 1	196 (8.5 %) Complex^a 140	810 (35.0 %) Complex^a 36
Polymorphic variations
\|ΔΔG\| ≤ 1	198 (55.6 %) Monomer^a 131	84 (23.6 %) Monomer^a 5
\|ΔΔG\| ≤ 1	186 (52.2 %) Complex^a 119	96 (27.0 %) Complex^a 17
\|ΔΔG\| > 1	29 (8.1 %) Monomer^a 21	45 (12.6 %) Monomer^a 9
\|ΔΔG\| > 1	29 (8.1 %) Complex^a 21	45 (12.6 %) Complex^a 9

^aNumber of residue predicted to be part of a protein-protein interaction patch. 2316 disease related variations and 356 polymorphic variations in 191 proteins. Predictions of INPS-3D and PRED-PPI are independent of the assembly state. RSA values were independently estimated on the monomeric and the complex structures