Dataset Information

Attention mechanism enhanced LSTM with residual architecture and its application for protein-protein interaction residue pairs prediction.

ABSTRACT: BACKGROUND:Recurrent neural network(RNN) is a good way to process sequential data, but the capability of RNN to compute long sequence data is inefficient. As a variant of RNN, long short term memory(LSTM) solved the problem in some extent. Here we improved LSTM for big data application in protein-protein interaction interface residue pairs prediction based on the following two reasons. On the one hand, there are some deficiencies in LSTM, such as shallow layers, gradient explosion or vanishing, etc. With a dramatic data increasing, the imbalance between algorithm innovation and big data processing has been more serious and urgent. On the other hand, protein-protein interaction interface residue pairs prediction is an important problem in biology, but the low prediction accuracy compels us to propose new computational methods. RESULTS:In order to surmount aforementioned problems of LSTM, we adopt the residual architecture and add attention mechanism to LSTM. In detail, we redefine the block, and add a connection from front to back in every two layers and attention mechanism to strengthen the capability of mining information. Then we use it to predict protein-protein interaction interface residue pairs, and acquire a quite good accuracy over 72%. What's more, we compare our method with random experiments, PPiPP, standard LSTM, and some other machine learning methods. Our method shows better performance than the methods mentioned above. CONCLUSION:We present an attention mechanism enhanced LSTM with residual architecture, and make deeper network without gradient vanishing or explosion to a certain extent. Then we apply it to a significant problem- protein-protein interaction interface residue pairs prediction and obtain a better accuracy than other methods. Our method provides a new approach for protein-protein interaction computation, which will be helpful for related biomedical researches.

SUBMITTER: Liu J

PROVIDER: S-EPMC6882172 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Attention mechanism enhanced LSTM with residual architecture and its application for protein-protein interaction residue pairs prediction.

Liu Jiale J Gong Xinqi X

BMC bioinformatics 20191127 1

<h4>Background</h4>Recurrent neural network(RNN) is a good way to process sequential data, but the capability of RNN to compute long sequence data is inefficient. As a variant of RNN, long short term memory(LSTM) solved the problem in some extent. Here we improved LSTM for big data application in protein-protein interaction interface residue pairs prediction based on the following two reasons. On the one hand, there are some deficiencies in LSTM, such as shallow layers, gradient explosion or van ...[more]

PMID: 31775612

Similar Datasets

Project description:Residue-residue interactions that fold a protein into a unique three-dimensional structure and make it play a specific function impose structural and functional constraints in varying degrees on each residue site. Selective constraints on residue sites are recorded in amino acid orders in homologous sequences and also in the evolutionary trace of amino acid substitutions. A challenge is to extract direct dependences between residue sites by removing phylogenetic correlations and indirect dependences through other residues within a protein or even through other molecules. Rapid growth of protein families with unknown folds requires an accurate de novo prediction method for protein structure. Recent attempts of disentangling direct from indirect dependences of amino acid types between residue positions in multiple sequence alignments have revealed that inferred residue-residue proximities can be sufficient information to predict a protein fold without the use of known three-dimensional structures. Here, we propose an alternative method of inferring coevolving site pairs from concurrent and compensatory substitutions between sites in each branch of a phylogenetic tree. Substitution probability and physico-chemical changes (volume, charge, hydrogen-bonding capability, and others) accompanied by substitutions at each site in each branch of a phylogenetic tree are estimated with the likelihood of each substitution, and their direct correlations between sites are used to detect concurrent and compensatory substitutions. In order to extract direct dependences between sites, partial correlation coefficients of the characteristic changes along branches between sites, in which linear multiple dependences on feature vectors at other sites are removed, are calculated and used to rank coevolving site pairs. Accuracy of contact prediction based on the present coevolution score is comparable to that achieved by a maximum entropy model of protein sequences for 15 protein families taken from the Pfam release 26.0. Besides, this excellent accuracy indicates that compensatory substitutions are significant in protein evolution.

Project description:BackgroundDriven by deep learning, inter-residue contact/distance prediction has been significantly improved and substantially enhanced ab initio protein structure prediction. Currently, most of the distance prediction methods classify inter-residue distances into multiple distance intervals instead of directly predicting real-value distances. The output of the former has to be converted into real-value distances to be used in tertiary structure prediction.ResultsTo explore the potentials of predicting real-value inter-residue distances, we develop a multi-task deep learning distance predictor (DeepDist) based on new residual convolutional network architectures to simultaneously predict real-value inter-residue distances and classify them into multiple distance intervals. Tested on 43 CASP13 hard domains, DeepDist achieves comparable performance in real-value distance prediction and multi-class distance prediction. The average mean square error (MSE) of DeepDist's real-value distance prediction is 0.896 Å2 when filtering out the predicted distance ≥ 16 Å, which is lower than 1.003 Å2 of DeepDist's multi-class distance prediction. When distance predictions are converted into contact predictions at 8 Å threshold (the standard threshold in the field), the precision of top L/5 and L/2 contact predictions of DeepDist's multi-class distance prediction is 79.3% and 66.1%, respectively, higher than 78.6% and 64.5% of its real-value distance prediction and the best results in the CASP13 experiment.ConclusionsDeepDist can predict inter-residue distances well and improve binary contact prediction over the existing state-of-the-art methods. Moreover, the predicted real-value distances can be directly used to reconstruct protein tertiary structures better than multi-class distance predictions due to the lower MSE. Finally, we demonstrate that predicting the real-value distance map and multi-class distance map at the same time performs better than predicting real-value distances alone.

Dataset Information

Attention mechanism enhanced LSTM with residual architecture and its application for protein-protein interaction residue pairs prediction.

Publications

Attention mechanism enhanced LSTM with residual architecture and its application for protein-protein interaction residue pairs prediction.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets