Background: Previous studies on protein-DNA interaction mostly focused on the bound structure of DNA-binding proteins but few paid enough attention to the unbound structures. As more new proteins are discovered, it is useful and imperative to develop algorithms for the functional prediction of unbound proteins. In our work, we apply an alpha shape model to represent the surface structure of the protein-DNA complex and extract useful statistical and geometric features, and use structural alignment and support vector machines for the prediction of unbound DNA-binding proteins.Results: The performance of our method is evaluated by discriminating a set of 104 DNA-binding proteins from 401 non-DNA-binding proteins. In the same test, the proposed method outperforms the other method using conditional probability. The results achieved by our proposed method for; precision, 83.33%; accuracy, 86.53%; and MCC, 0.5368 demonstrate its good performance.Conclusions: In this study we develop an effective method for the prediction of protein-DNA interactions based on statistical and geometric features and support vector machines. Our results show that interface surface features play an important role in protein-DNA interaction. Our technique is able to predict unbound DNA-binding protein and discriminatory DNA-binding proteins from proteins that bind with other molecules.
ASJC Scopus subject areas
- Molecular Biology