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      IonchanPred 2.0: A Tool to Predict Ion Channels and Their Types

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          Abstract

          Ion channels (IC) are ion-permeable protein pores located in the lipid membranes of all cells. Different ion channels have unique functions in different biological processes. Due to the rapid development of high-throughput mass spectrometry, proteomic data are rapidly accumulating and provide us an opportunity to systematically investigate and predict ion channels and their types. In this paper, we constructed a support vector machine (SVM)-based model to quickly predict ion channels and their types. By considering the residue sequence information and their physicochemical properties, a novel feature-extracted method which combined dipeptide composition with the physicochemical correlation between two residues was employed. A feature selection strategy was used to improve the performance of the model. Comparison results of in jackknife cross-validation demonstrated that our method was superior to other methods for predicting ion channels and their types. Based on the model, we built a web server called IonchanPred which can be freely accessed from http://lin.uestc.edu.cn/server/IonchanPredv2.0.

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          Most cited references34

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          Cryo-electron microscopy structure of the TRPV2 ion channel

          Transient receptor potential vanilloid (TRPV) cation channels are polymodal sensors involved in a variety of physiological processes. TRPV2, a member of the TRPV family, is regulated by temperature, by ligands, such as probenecid and cannabinoids, and by lipids. TRPV2 has been implicated in many biological functions, including somatosensation, osmosensation and innate immunity. Here we present the atomic model of rabbit TRPV2 in its putative desensitized state, as determined by cryo-EM at a nominal resolution of ~4 Å. In the TRPV2 structure, the transmembrane segment 6 (S6), which is involved in gate opening, adopts a conformation different from the one observed in TRPV1. Structural comparisons of TRPV1 and TRPV2 indicate that a rotation of the ankyrin-repeat domain is coupled to pore opening via the TRP domain, and this pore opening can be modulated by rearrangements in the secondary structure of S6.
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            PseAAC: a flexible web server for generating various kinds of protein pseudo amino acid composition.

            The pseudo amino acid (PseAA) composition can represent a protein sequence in a discrete model without completely losing its sequence-order information, and hence has been widely applied for improving the prediction quality for various protein attributes. However, dealing with different problems may need different kinds of PseAA composition. Here, we present a web-server called PseAAC at http://chou.med.harvard.edu/bioinf/PseAA/, by which users can generate various kinds of PseAA composition to best fit their need.
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              Combining evolutionary information extracted from frequency profiles with sequence-based kernels for protein remote homology detection

              Abstract Motivation: Owing to its importance in both basic research (such as molecular evolution and protein attribute prediction) and practical application (such as timely modeling the 3D structures of proteins targeted for drug development), protein remote homology detection has attracted a great deal of interest. It is intriguing to note that the profile-based approach is promising and holds high potential in this regard. To further improve protein remote homology detection, a key step is how to find an optimal means to extract the evolutionary information into the profiles. Results: Here, we propose a novel approach, the so-called profile-based protein representation, to extract the evolutionary information via the frequency profiles. The latter can be calculated from the multiple sequence alignments generated by PSI-BLAST. Three top performing sequence-based kernels (SVM-Ngram, SVM-pairwise and SVM-LA) were combined with the profile-based protein representation. Various tests were conducted on a SCOP benchmark dataset that contains 54 families and 23 superfamilies. The results showed that the new approach is promising, and can obviously improve the performance of the three kernels. Furthermore, our approach can also provide useful insights for studying the features of proteins in various families. It has not escaped our notice that the current approach can be easily combined with the existing sequence-based methods so as to improve their performance as well. Availability and implementation: For users’ convenience, the source code of generating the profile-based proteins and the multiple kernel learning was also provided at http://bioinformatics.hitsz.edu.cn/main/∼binliu/remote/ Contact: bliu@insun.hit.edu.cn or bliu@gordonlifescience.org Supplementary information: Supplementary data are available at Bioinformatics online.
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                Author and article information

                Journal
                Int J Mol Sci
                Int J Mol Sci
                ijms
                International Journal of Molecular Sciences
                MDPI
                1422-0067
                24 August 2017
                September 2017
                : 18
                : 9
                : 1838
                Affiliations
                [1 ]Key Laboratory for Neuro-Information of Ministry of Education, School of Life Science and Technology, Center for Informational Biology, University of Electronic Science and Technology of China, Chengdu 610054, China; lianyingteng@ 123456hotmail.com (Y.-W.Z.); zhendong_su@ 123456163.com (Z.-D.S.); wyang@ 123456imu.edu.cn (W.Y.)
                [2 ]Development and Planning Department, Inner Mongolia University, Hohhot 010021, China
                [3 ]Department of Physics, School of Sciences, and Center for Genomics and Computational Biology, North China University of Science and Technology, Tangshan 063000, China
                [4 ]Department of Pathophysiology, Southwest Medical University, Luzhou 646000, China
                Author notes
                [* ]Correspondence: hlin@ 123456uestc.edu.cn (H.L.); greatchen@ 123456ncst.edu.cn (W.C.); tanghua771211@ 123456aliyun.com (H.T.); Tel.: +86-28-8320-2351 (H.L. & W.C. & H.T.)
                Author information
                https://orcid.org/0000-0001-6265-2862
                Article
                ijms-18-01838
                10.3390/ijms18091838
                5618487
                28837067
                25c820ea-b90c-4c13-bec4-cad4b873936a
                © 2017 by the authors.

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                : 07 August 2017
                : 21 August 2017
                Categories
                Article

                Molecular biology
                ion channels,pseudo-dipeptide composition,machine learning method
                Molecular biology
                ion channels, pseudo-dipeptide composition, machine learning method

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