Dataset Information

Accurate prediction of protein relative solvent accessibility using a balanced model.

ABSTRACT: BACKGROUND:Protein relative solvent accessibility provides insight into understanding protein structure and function. Prediction of protein relative solvent accessibility is often the first stage of predicting other protein properties. Recent predictors of relative solvent accessibility discriminate against exposed regions as compared with buried regions, resulting in higher prediction accuracy associated with buried regions relative to exposed regions. METHODS:Here, we propose a more accurate and balanced predictor of protein relative solvent accessibility. First, we collected known proteins in three subsets according to sequence length and constructed a balanced dataset after reducing redundancy within each subset. Next, we measured the performance associated with different variables and variable combinations to determine the best variable combination. Finally, a predictor called BMRSA was constructed for modelling and prediction, which used the balanced set as the training set, the position- specific scoring matrix, predicted secondary structure, buried-exposed profile, and length of a query sequence as variables, and the conditional random field as the machine-learning method. RESULTS:BMRSA performance on test sets confirmed that our approach improved prediction accuracy relative to state-of-the-art approaches and was balanced in its comparison of buried and exposed regions. Our method is valuable when higher levels of accuracy in predicting exposed-residue states are required. The BMRSA is available at: http://cheminfo.tongji.edu.cn:8080/BMRSA/.

SUBMITTER: Wu W

PROVIDER: S-EPMC5259893 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature

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Accurate prediction of protein relative solvent accessibility using a balanced model.

Wu Wei W Wang Zhiheng Z Cong Peisheng P Li Tonghua T

BioData mining 20170124

<h4>Background</h4>Protein relative solvent accessibility provides insight into understanding protein structure and function. Prediction of protein relative solvent accessibility is often the first stage of predicting other protein properties. Recent predictors of relative solvent accessibility discriminate against exposed regions as compared with buried regions, resulting in higher prediction accuracy associated with buried regions relative to exposed regions.<h4>Methods</h4>Here, we propose a ...[more]

PMID: 28127402

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Project description:BACKGROUND: It is well known that most of the binding free energy of protein interaction is contributed by a few key hot spot residues. These residues are crucial for understanding the function of proteins and studying their interactions. Experimental hot spots detection methods such as alanine scanning mutagenesis are not applicable on a large scale since they are time consuming and expensive. Therefore, reliable and efficient computational methods for identifying hot spots are greatly desired and urgently required. RESULTS: In this work, we introduce an efficient approach that uses support vector machine (SVM) to predict hot spot residues in protein interfaces. We systematically investigate a wide variety of 62 features from a combination of protein sequence and structure information. Then, to remove redundant and irrelevant features and improve the prediction performance, feature selection is employed using the F-score method. Based on the selected features, nine individual-feature based predictors are developed to identify hot spots using SVMs. Furthermore, a new ensemble classifier, namely APIS (A combined model based on Protrusion Index and Solvent accessibility), is developed to further improve the prediction accuracy. The results on two benchmark datasets, ASEdb and BID, show that this proposed method yields significantly better prediction accuracy than those previously published in the literature. In addition, we also demonstrate the predictive power of our proposed method by modelling two protein complexes: the calmodulin/myosin light chain kinase complex and the heat shock locus gene products U and V complex, which indicate that our method can identify more hot spots in these two complexes compared with other state-of-the-art methods. CONCLUSION: We have developed an accurate prediction model for hot spot residues, given the structure of a protein complex. A major contribution of this study is to propose several new features based on the protrusion index of amino acid residues, which has been shown to significantly improve the prediction performance of hot spots. Moreover, we identify a compact and useful feature subset that has an important implication for identifying hot spot residues. Our results indicate that these features are more effective than the conventional evolutionary conservation, pairwise residue potentials and other traditional features considered previously, and that the combination of our and traditional features may support the creation of a discriminative feature set for efficient prediction of hot spot residues. The data and source code are available on web site http://home.ustc.edu.cn/~jfxia/hotspot.html.

Dataset Information

Accurate prediction of protein relative solvent accessibility using a balanced model.

Publications

Accurate prediction of protein relative solvent accessibility using a balanced model.

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