Inferring Protein-Protein Interacting Sites Using Residue Conservation and Evolutionary Information
This paper proposes a novel method using protein residue conservation and evolution information, i.e., spatial sequence profile, sequence information entropy and evolution rate, to infer protein binding sites. Some predictors based on support vector machines (SVMs) algorithm are constructed to predict the role of surface residues in protein-protein interface. By combining protein residue characters, the prediction performance can be improved obviously. We then made use of the predicted labels of neighbor residues to improve the performance of the predictors. The efficiency and the effectiveness of our proposed approach are verified by its better prediction performance based on a non-redundant data set of heterodimers.
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Document Type: Research Article
Affiliations: Hefei Institute Intelligent Machines, Chinese Academy of Science, Hefei, Anhui, 230031, China.
Publication date: 2006-10-01
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- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.