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      HMMBinder: DNA-Binding Protein Prediction Using HMM Profile Based Features

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          Abstract

          DNA-binding proteins often play important role in various processes within the cell. Over the last decade, a wide range of classification algorithms and feature extraction techniques have been used to solve this problem. In this paper, we propose a novel DNA-binding protein prediction method called HMMBinder. HMMBinder uses monogram and bigram features extracted from the HMM profiles of the protein sequences. To the best of our knowledge, this is the first application of HMM profile based features for the DNA-binding protein prediction problem. We applied Support Vector Machines (SVM) as a classification technique in HMMBinder. Our method was tested on standard benchmark datasets. We experimentally show that our method outperforms the state-of-the-art methods found in the literature.

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          Most cited references38

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          Analysis and prediction of DNA-binding proteins and their binding residues based on composition, sequence and structural information.

          Though vitally important to cell function, the mechanism of protein-DNA binding has not yet been completely understood. We therefore analysed the relationship between DNA binding and protein sequence composition, solvent accessibility and secondary structure. Using non-redundant databases of transcription factors and protein-DNA complexes, neural network models were developed to utilize the information present in this relationship to predict DNA-binding proteins and their binding residues. Sequence composition was found to provide sufficient information to predict the probability of its binding to DNA with nearly 69% sensitivity at 64% accuracy for the considered proteins; sequence neighbourhood and solvent accessibility information were sufficient to make binding site predictions with 40% sensitivity at 79% accuracy. Detailed analysis of binding residues shows that some three- and five-residue segments frequently bind to DNA and that solvent accessibility plays a major role in binding. Although, binding behaviour was not associated with any particular secondary structure, there were interesting exceptions at the residue level. Over-representation of some residues in the binding sites was largely lost at the total sequence level, but a different kind of compositional preference was observed in DNA-binding proteins.
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            Local-DPP: An improved DNA-binding protein prediction method by exploring local evolutionary information

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              An overview of the structures of protein-DNA complexes

              On the basis of a structural analysis of 240 protein-DNA complexes contained in the Protein Data Bank (PDB), we have classified the DNA-binding proteins involved into eight different structural/functional groups, which are further classified into 54 structural families. Here we present this classification and review the functions, structures and binding interactions of these protein-DNA complexes.
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                Author and article information

                Contributors
                Journal
                Biomed Res Int
                Biomed Res Int
                BMRI
                BioMed Research International
                Hindawi
                2314-6133
                2314-6141
                2017
                14 November 2017
                : 2017
                : 4590609
                Affiliations
                1Department of Computer Science and Engineering, United International University, Dhaka, Bangladesh
                2School of Computing, Information and Mathematical Sciences, The University of the South Pacific, Suva, Fiji
                3Institute for Integrated and Intelligent Systems, Griffith University, Brisbane, QLD, Australia
                4School of Engineering and Physics, The University of the South Pacific, Suva, Fiji
                5RIKEN Center for Integrative Medical Sciences, Yokohama, Japan
                6Department of Computer Science, Morgan State University, Baltimore, MD, USA
                Author notes

                Academic Editor: Paul Harrison

                Author information
                http://orcid.org/0000-0001-9919-5482
                http://orcid.org/0000-0003-3347-2381
                http://orcid.org/0000-0003-0669-072X
                Article
                10.1155/2017/4590609
                5706079
                29270430
                c5f54254-8671-4fac-ae5c-5087d789254e
                Copyright © 2017 Rianon Zaman et al.

                This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                : 29 August 2017
                : 22 October 2017
                Categories
                Research Article

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