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A novel matrix of sequence descriptors for predicting protein-protein interactions from amino acid sequences.

ABSTRACT: Protein-protein interactions (PPIs) play an important role in the life activities of organisms. With the availability of large amounts of protein sequence data, PPIs prediction methods have attracted increasing attention. A variety of protein sequence coding methods have emerged, but the training of these methods is particularly time consuming. To solve this issue, we have proposed a novel matrix sequence coding method. Based on deep neural network (DNN) and a novel matrix protein sequence descriptor, we constructed a protein interaction prediction model for predicting PPIs. When performed on human PPIs data, the method achieved an accuracy of 94.34%, a recall of 98.28%, an area under the curve (AUC) of 97.79% and a loss of 23.25%. A non-redundant dataset was used to evaluate this prediction model, and the prediction accuracy is 88.29%. These results indicate that the matrix of sequence (MOS) descriptor can enhance the predictive power of PPIs and reduce training time, which can be a useful complement for future proteomics research. The experimental code and experimental results can be found at https://github.com/smalltalkman/hppi-tensorflow.

SUBMITTER: Wang X

PROVIDER: S-EPMC6555512 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature

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A novel matrix of sequence descriptors for predicting protein-protein interactions from amino acid sequences.

Wang Xue X Wu Yuejin Y Wang Rujing R Wei Yuanyuan Y Gui Yuanmiao Y

PloS one 20190607 6

Protein-protein interactions (PPIs) play an important role in the life activities of organisms. With the availability of large amounts of protein sequence data, PPIs prediction methods have attracted increasing attention. A variety of protein sequence coding methods have emerged, but the training of these methods is particularly time consuming. To solve this issue, we have proposed a novel matrix sequence coding method. Based on deep neural network (DNN) and a novel matrix protein sequence descr ...[more]

PMID: 31173605

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Project description:Protein-protein interactions (PPIs) are involved in various biological processes, and underlying mechanism of the interactions plays a crucial role in therapeutics and protein engineering. Most machine learning approaches have been developed for predicting the binding affinity of protein-protein complexes based on structure and functional information. This work aims to predict the binding affinity of heterodimeric protein complexes from sequences only.This work proposes a support vector machine (SVM) based binding affinity classifier, called SVM-BAC, to classify heterodimeric protein complexes based on the prediction of their binding affinity. SVM-BAC identified 14 of 580 sequence descriptors (physicochemical, energetic and conformational properties of the 20 amino acids) to classify 216 heterodimeric protein complexes into low and high binding affinity. SVM-BAC yielded the training accuracy, sensitivity, specificity, AUC and test accuracy of 85.80%, 0.89, 0.83, 0.86 and 83.33%, respectively, better than existing machine learning algorithms. The 14 features and support vector regression were further used to estimate the binding affinities (Pkd) of 200 heterodimeric protein complexes. Prediction performance of a Jackknife test was the correlation coefficient of 0.34 and mean absolute error of 1.4. We further analyze three informative physicochemical properties according to their contribution to prediction performance. Results reveal that the following properties are effective in predicting the binding affinity of heterodimeric protein complexes: apparent partition energy based on buried molar fractions, relations between chemical structure and biological activity in principal component analysis IV, and normalized frequency of beta turn.The proposed sequence-based prediction method SVM-BAC uses an optimal feature selection method to identify 14 informative features to classify and predict binding affinity of heterodimeric protein complexes. The characterization analysis revealed that the average numbers of beta turns and hydrogen bonds at protein-protein interfaces in high binding affinity complexes are more than those in low binding affinity complexes.

Dataset Information

A novel matrix of sequence descriptors for predicting protein-protein interactions from amino acid sequences.

Publications

A novel matrix of sequence descriptors for predicting protein-protein interactions from amino acid sequences.

Similar Datasets

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