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TMFoldWeb: a web server for predicting transmembrane protein fold class

BACKGROUND: Here we present TMFoldWeb, the web server implementation of TMFoldRec, a transmembrane protein fold recognition algorithm. TMFoldRec uses statistical potentials and utilizes topology filtering and a gapless threading algorithm. It ranks template structures and selects the most likely can...

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Autores principales: Kozma, Dániel, Tusnády, Gábor E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4574079/
https://www.ncbi.nlm.nih.gov/pubmed/26381605
http://dx.doi.org/10.1186/s13062-015-0082-5
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author Kozma, Dániel
Tusnády, Gábor E.
author_facet Kozma, Dániel
Tusnády, Gábor E.
author_sort Kozma, Dániel
collection PubMed
description BACKGROUND: Here we present TMFoldWeb, the web server implementation of TMFoldRec, a transmembrane protein fold recognition algorithm. TMFoldRec uses statistical potentials and utilizes topology filtering and a gapless threading algorithm. It ranks template structures and selects the most likely candidates and estimates the reliability of the obtained lowest energy model. The statistical potential was developed in a maximum likelihood framework on a representative set of the PDBTM database. According to the benchmark test the performance of TMFoldRec is about 77 % in correctly predicting fold class for a given transmembrane protein sequence. RESULTS: An intuitive web interface has been developed for the recently published TMFoldRec algorithm. The query sequence goes through a pipeline of topology prediction and a systematic sequence to structure alignment (threading). Resulting templates are ordered by energy and reliability values and are colored according to their significance level. Besides the graphical interface, a programmatic access is available as well, via a direct interface for developers or for submitting genome-wide data sets. CONCLUSIONS: The TMFoldWeb web server is unique and currently the only web server that is able to predict the fold class of transmembrane proteins while assigning reliability scores for the prediction. This method is prepared for genome-wide analysis with its easy-to-use interface, informative result page and programmatic access. Considering the info-communication evolution in the last few years, the developed web server, as well as the molecule viewer, is responsive and fully compatible with the prevalent tablets and mobile devices. REVIEWERS: This article was reviewed by Dr. Michael Gromiha, Dr. Sandor Pongor and Dr. Frank Eisenhaber with Wing-Cheong Wong.
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spelling pubmed-45740792015-09-19 TMFoldWeb: a web server for predicting transmembrane protein fold class Kozma, Dániel Tusnády, Gábor E. Biol Direct Application Note BACKGROUND: Here we present TMFoldWeb, the web server implementation of TMFoldRec, a transmembrane protein fold recognition algorithm. TMFoldRec uses statistical potentials and utilizes topology filtering and a gapless threading algorithm. It ranks template structures and selects the most likely candidates and estimates the reliability of the obtained lowest energy model. The statistical potential was developed in a maximum likelihood framework on a representative set of the PDBTM database. According to the benchmark test the performance of TMFoldRec is about 77 % in correctly predicting fold class for a given transmembrane protein sequence. RESULTS: An intuitive web interface has been developed for the recently published TMFoldRec algorithm. The query sequence goes through a pipeline of topology prediction and a systematic sequence to structure alignment (threading). Resulting templates are ordered by energy and reliability values and are colored according to their significance level. Besides the graphical interface, a programmatic access is available as well, via a direct interface for developers or for submitting genome-wide data sets. CONCLUSIONS: The TMFoldWeb web server is unique and currently the only web server that is able to predict the fold class of transmembrane proteins while assigning reliability scores for the prediction. This method is prepared for genome-wide analysis with its easy-to-use interface, informative result page and programmatic access. Considering the info-communication evolution in the last few years, the developed web server, as well as the molecule viewer, is responsive and fully compatible with the prevalent tablets and mobile devices. REVIEWERS: This article was reviewed by Dr. Michael Gromiha, Dr. Sandor Pongor and Dr. Frank Eisenhaber with Wing-Cheong Wong. BioMed Central 2015-09-17 /pmc/articles/PMC4574079/ /pubmed/26381605 http://dx.doi.org/10.1186/s13062-015-0082-5 Text en © Kozma and Tusnády. 2015 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Application Note
Kozma, Dániel
Tusnády, Gábor E.
TMFoldWeb: a web server for predicting transmembrane protein fold class
title TMFoldWeb: a web server for predicting transmembrane protein fold class
title_full TMFoldWeb: a web server for predicting transmembrane protein fold class
title_fullStr TMFoldWeb: a web server for predicting transmembrane protein fold class
title_full_unstemmed TMFoldWeb: a web server for predicting transmembrane protein fold class
title_short TMFoldWeb: a web server for predicting transmembrane protein fold class
title_sort tmfoldweb: a web server for predicting transmembrane protein fold class
topic Application Note
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4574079/
https://www.ncbi.nlm.nih.gov/pubmed/26381605
http://dx.doi.org/10.1186/s13062-015-0082-5
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