Identifying protein-protein interfacial residues in heterocomplexes using residue conservation scores.

Identifying protein-protein interfaces is crucial for structural biology. Because of the constraints in wet experiments, many computational methods have been proposed. Without knowing any information about the partner chains, a new method of predicting protein-protein interaction interface residues purely based on evolutionary information in heterocomplexes is proposed here. Unlike traditional approaches using multiple sequence alignment profiles to represent the conservation level for each residue, we make predictions based on the concept of residue conservation scores so that the dimension of the feature vector for each residue can be drastically reduced, at least 20 times less than conventional methods. Based on the representation approach, a simple linear discriminant function is used to make predictions, so the computational complexity of the whole prediction procedure can also be greatly decreased. By testing our approach on 69 heterocomplex chains, experimental results demonstrate the performance of our approach is indeed superior to current existing methods.