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FEGS: a novel feature extraction model for protein sequences and its applications
BACKGROUND: Feature extraction of protein sequences is widely used in various research areas related to protein analysis, such as protein similarity analysis and prediction of protein functions or interactions. RESULTS: In this study, we introduce FEGS (Feature Extraction based on Graphical and Stat...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8172329/ https://www.ncbi.nlm.nih.gov/pubmed/34078264 http://dx.doi.org/10.1186/s12859-021-04223-3 |
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author | Mu, Zengchao Yu, Ting Liu, Xiaoping Zheng, Hongyu Wei, Leyi Liu, Juntao |
author_facet | Mu, Zengchao Yu, Ting Liu, Xiaoping Zheng, Hongyu Wei, Leyi Liu, Juntao |
author_sort | Mu, Zengchao |
collection | PubMed |
description | BACKGROUND: Feature extraction of protein sequences is widely used in various research areas related to protein analysis, such as protein similarity analysis and prediction of protein functions or interactions. RESULTS: In this study, we introduce FEGS (Feature Extraction based on Graphical and Statistical features), a novel feature extraction model of protein sequences, by developing a new technique for graphical representation of protein sequences based on the physicochemical properties of amino acids and effectively employing the statistical features of protein sequences. By fusing the graphical and statistical features, FEGS transforms a protein sequence into a 578-dimensional numerical vector. When FEGS is applied to phylogenetic analysis on five protein sequence data sets, its performance is notably better than all of the other compared methods. CONCLUSION: The FEGS method is carefully designed, which is practically powerful for extracting features of protein sequences. The current version of FEGS is developed to be user-friendly and is expected to play a crucial role in the related studies of protein sequence analyses. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s12859-021-04223-3. |
format | Online Article Text |
id | pubmed-8172329 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-81723292021-06-03 FEGS: a novel feature extraction model for protein sequences and its applications Mu, Zengchao Yu, Ting Liu, Xiaoping Zheng, Hongyu Wei, Leyi Liu, Juntao BMC Bioinformatics Research BACKGROUND: Feature extraction of protein sequences is widely used in various research areas related to protein analysis, such as protein similarity analysis and prediction of protein functions or interactions. RESULTS: In this study, we introduce FEGS (Feature Extraction based on Graphical and Statistical features), a novel feature extraction model of protein sequences, by developing a new technique for graphical representation of protein sequences based on the physicochemical properties of amino acids and effectively employing the statistical features of protein sequences. By fusing the graphical and statistical features, FEGS transforms a protein sequence into a 578-dimensional numerical vector. When FEGS is applied to phylogenetic analysis on five protein sequence data sets, its performance is notably better than all of the other compared methods. CONCLUSION: The FEGS method is carefully designed, which is practically powerful for extracting features of protein sequences. The current version of FEGS is developed to be user-friendly and is expected to play a crucial role in the related studies of protein sequence analyses. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s12859-021-04223-3. BioMed Central 2021-06-03 /pmc/articles/PMC8172329/ /pubmed/34078264 http://dx.doi.org/10.1186/s12859-021-04223-3 Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/ (https://creativecommons.org/publicdomain/zero/1.0/) ) applies to the data made available in this article, unless otherwise stated in a credit line to the data. |
spellingShingle | Research Mu, Zengchao Yu, Ting Liu, Xiaoping Zheng, Hongyu Wei, Leyi Liu, Juntao FEGS: a novel feature extraction model for protein sequences and its applications |
title | FEGS: a novel feature extraction model for protein sequences and its applications |
title_full | FEGS: a novel feature extraction model for protein sequences and its applications |
title_fullStr | FEGS: a novel feature extraction model for protein sequences and its applications |
title_full_unstemmed | FEGS: a novel feature extraction model for protein sequences and its applications |
title_short | FEGS: a novel feature extraction model for protein sequences and its applications |
title_sort | fegs: a novel feature extraction model for protein sequences and its applications |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8172329/ https://www.ncbi.nlm.nih.gov/pubmed/34078264 http://dx.doi.org/10.1186/s12859-021-04223-3 |
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