A novel method of predicting protein disordered regions based on sequence features

14Citations
Citations of this article
21Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

With a large number of disordered proteins and their important functions discovered, it is highly desired to develop effective methods to computationally predict protein disordered regions. In this study, based on Random Forest (RF), Maximum Relevancy Minimum Redundancy (mRMR), and Incremental Feature Selection (IFS), we developed a new method to predict disordered regions in proteins. The mRMR criterion was used to rank the importance of all candidate features. Finally, top 128 features were selected from the ranked feature list to build the optimal model, including 92 Position Specific Scoring Matrix (PSSM) conservation score features and 36 secondary structure features. As a result, Matthews correlation coefficient (MCC) of 0.3895 was achieved on the training set by 10-fold cross-validation. On the basis of predicting results for each query sequence by using the method, we used the scanning and modification strategy to improve the performance. The accuracy (ACC) and MCC were increased by 4% and almost 0.2%, respectively, compared with other three popular predictors: DISOPRED, DISOclust, and OnD-CRF. The selected features may shed some light on the understanding of the formation mechanism of disordered structures, providing guidelines for experimental validation. © 2013 Tong-Hui Zhao et al.

Cite

CITATION STYLE

APA

Zhao, T. H., Jiang, M., Huang, T., Li, B. Q., Zhang, N., Li, H. P., & Cai, Y. D. (2013). A novel method of predicting protein disordered regions based on sequence features. BioMed Research International, 2013. https://doi.org/10.1155/2013/414327

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free