Sequence-based identification of interface residues by an integrative profile combining hydrophobic and evolutionary information.

ABSTRACT:

Background

Protein-protein interactions play essential roles in protein function determination and drug design. Numerous methods have been proposed to recognize their interaction sites, however, only a small proportion of protein complexes have been successfully resolved due to the high cost. Therefore, it is important to improve the performance for predicting protein interaction sites based on primary sequence alone.

Results

We propose a new idea to construct an integrative profile for each residue in a protein by combining its hydrophobic and evolutionary information. A support vector machine (SVM) ensemble is then developed, where SVMs train on different pairs of positive (interface sites) and negative (non-interface sites) subsets. The subsets having roughly the same siz

SUBMITTER: Chen P 

PROVIDER: S-EPMC2921408 | biostudies-literature | 2010 Jul

REPOSITORIES: biostudies-literature