A simple and efficient method for predicting protein-protein interaction sites.

Enter multiple e-mails separated by comma.

imagem

Author(s): HIGA, R. H.; TOZZI, C. L.

Summary: Computational methods for predicting protein-protein interaction sites based on structural data are characterized by an accuracy between 70 and 80%. Some experimental studies indicate that only a fraction of the residues, forming clusters in the center of the interaction site, are energetically important for binding. In addition, the analysis of amino acid composition has shown that residues located in the center of the interaction site can be better discriminated from the residues in other parts of the protein surface. In the present study, we implement a simple method to predict interaction site residues exploiting this fact and show that it achieves a very competitive performance compared to other methods using the same dataset and criteria for performance evaluation (success rate of 82.1%).

Publication year: 2008

Types of publication: Journal article

Observation

Some of Embrapa's publications are published as ePub files. To read them, use or download one of the following free software options to your computer or mobile device. Android: Google Play Books; IOS: iBooks; Windows and Linux: Calibre.

 


Access other publications

Access the Agricultural Research Database (BDPA) to consult Embrapa's full library collection and records.
Visit Embrapa Bookstore to purchase books and other publications sold by Embrapa.