Table 2.
Pearson's correlations and p-values between experimental binding affinities and the inter-residue contacts (ICs), buried surface area (BSA) and non-interacting surface (NIS) (Kastritis et al., 2014) properties calculated on the ‘cleaned’ dataset
| Property | R | p-value |
|---|---|---|
| ICs_total | −0.59 | <0.0001 |
| ICs_charged/charged | −0.17 | =0.06 |
| ICs_charged/polar | −0.26 | =0.009 |
| ICs_charged/apolar | −0.45 | <0.0001 |
| ICs_polar/polar | −0.13 | =0.1 |
| ICs_polar/apolar | −0.56 | <0.0001 |
| ICs_apolar/apolar | −0.34 | =0.001 |
| ICs_hydrophilic/hydrophilic | −0.53 | <0.0001 |
| ICs_hydrophilic/hydrophobic | −0.34 | =0.001 |
| ICs_hydrophobic/hydrophilic | −0.05 | =0.3 |
| BSA_total | −0.46 | <0.0001 |
| BSA_polar | −0.36 | =0.0005 |
| BSA_apolar | −0.47 | <0.0001 |
| %NIS_polar | 0.07 | =0.06 |
| %NIS_apolar | −0.33 | =0.001 |
| %NIS_charged | 0.28 | =0.006 |
A fine classification of those properties based on the polar/apolar/charged and hydrophobic/hydrophilic nature of the amino acids is also reported. The property with the highest R value is highlighted in bold. The corresponding data are provided in Supplementary file 2.