HSEpred: predict Half-Sphere Exposure from protein sequences

Bioinformatics Center, Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan.
Bioinformatics (Impact Factor: 4.62). 08/2008; 24(13):1489-97. DOI: 10.1093/bioinformatics/btn222
Source: PubMed


Half-sphere exposure (HSE) is a newly developed two-dimensional solvent exposure measure. By conceptually separating an amino acid's sphere in a protein structure into two half spheres which represent its distinct spatial neighborhoods in the upward and downward directions, the HSE-up and HSE-down measures show superior performance compared with other measures such as accessible surface area, residue depth and contact number. However, currently there is no existing method for the prediction of HSE measures from sequence data.
In this article, we propose a novel approach to predict the HSE measures and infer residue contact numbers using the predicted HSE values, based on a well-prepared non-homologous protein structure dataset. In particular, we employ support vector regression (SVR) to quantify the relationship between HSE measures and protein sequences and evaluate its prediction performance. We extensively explore five sequence-encoding schemes to examine their effects on the prediction performance. Our method could achieve the correlation coefficients of 0.72 and 0.68 between the predicted and observed HSE-up and HSE-down measures, respectively. Moreover, contact number can be accurately predicted by the summation of the predicted HSE-up and HSE-down values, which has further enlarged the application of this method. The successful application of SVR approach in this study suggests that it should be more useful in quantifying the protein sequence-structure relationship and predicting the structural property profiles from protein sequences.
The prediction webserver and supplementary materials are accessible at
Supplementary data are available at Bioinformatics online.

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Available from: Jiangning Song
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    • "The performance of SVM is largely dependent on the quality of the features (Liu et al., 2008). Although, plenty of feature representation and selection methods were proposed for protein sequence (Fang et al., 2008; Chou, 2011; Yuan et al., 2010; Song et al., 2008) and these methods were systematically surveyed (Nanni et al., 2010; Zhang et al., 2005), the underlying principle of protein-DNA interaction is still largely unknown. To this end, we propose a comprehensive feature representation, including the sequence information, evolutionary profiles, predicted secondary structural, predict relative solvent accessibility (RSA) information, physicochemical properties, and biological function information. "
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