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Harnessing the evolutionary information on oxygen binding proteins through Support Vector Machines based modules
OBJECTIVES: The arrival of free oxygen on the globe, aerobic life is becoming possible. However, it has become very clear that the oxygen binding proteins are widespread in the biosphere and are found in all groups of organisms, including prokaryotes, eukaryotes as well as in fungi, plants, and anim...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5948687/ https://www.ncbi.nlm.nih.gov/pubmed/29751818 http://dx.doi.org/10.1186/s13104-018-3383-9 |
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author | Muthukrishnan, Selvaraj Puri, Munish |
author_facet | Muthukrishnan, Selvaraj Puri, Munish |
author_sort | Muthukrishnan, Selvaraj |
collection | PubMed |
description | OBJECTIVES: The arrival of free oxygen on the globe, aerobic life is becoming possible. However, it has become very clear that the oxygen binding proteins are widespread in the biosphere and are found in all groups of organisms, including prokaryotes, eukaryotes as well as in fungi, plants, and animals. The exponential growth and availability of fresh annotated protein sequences in the databases motivated us to develop an improved version of “Oxypred” for identifying oxygen-binding proteins. RESULTS: In this study, we have proposed a method for identifying oxy-proteins with two different sequence similarity cutoffs 50 and 90%. A different amino acid composition based Support Vector Machines models was developed, including the evolutionary profiles in the form position-specific scoring matrix (PSSM). The fivefold cross-validation techniques were applied to evaluate the prediction performance. Also, we compared with existing methods, which shows nearly 97% recognition, but, our newly developed models were able to recognize almost 99.99 and 100% in both oxy-50 and 90% similarity models respectively. Our result shows that our approaches are faster and achieve a better prediction performance over the existing methods. The web-server Oxypred2 was developed for an alternative method for identifying oxy-proteins with more additional modules including PSSM, available at http://bioinfo.imtech.res.in/servers/muthu/oxypred2/home.html. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s13104-018-3383-9) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-5948687 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-59486872018-05-17 Harnessing the evolutionary information on oxygen binding proteins through Support Vector Machines based modules Muthukrishnan, Selvaraj Puri, Munish BMC Res Notes Research Note OBJECTIVES: The arrival of free oxygen on the globe, aerobic life is becoming possible. However, it has become very clear that the oxygen binding proteins are widespread in the biosphere and are found in all groups of organisms, including prokaryotes, eukaryotes as well as in fungi, plants, and animals. The exponential growth and availability of fresh annotated protein sequences in the databases motivated us to develop an improved version of “Oxypred” for identifying oxygen-binding proteins. RESULTS: In this study, we have proposed a method for identifying oxy-proteins with two different sequence similarity cutoffs 50 and 90%. A different amino acid composition based Support Vector Machines models was developed, including the evolutionary profiles in the form position-specific scoring matrix (PSSM). The fivefold cross-validation techniques were applied to evaluate the prediction performance. Also, we compared with existing methods, which shows nearly 97% recognition, but, our newly developed models were able to recognize almost 99.99 and 100% in both oxy-50 and 90% similarity models respectively. Our result shows that our approaches are faster and achieve a better prediction performance over the existing methods. The web-server Oxypred2 was developed for an alternative method for identifying oxy-proteins with more additional modules including PSSM, available at http://bioinfo.imtech.res.in/servers/muthu/oxypred2/home.html. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s13104-018-3383-9) contains supplementary material, which is available to authorized users. BioMed Central 2018-05-11 /pmc/articles/PMC5948687/ /pubmed/29751818 http://dx.doi.org/10.1186/s13104-018-3383-9 Text en © The Author(s) 2018 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 | Research Note Muthukrishnan, Selvaraj Puri, Munish Harnessing the evolutionary information on oxygen binding proteins through Support Vector Machines based modules |
title | Harnessing the evolutionary information on oxygen binding proteins through Support Vector Machines based modules |
title_full | Harnessing the evolutionary information on oxygen binding proteins through Support Vector Machines based modules |
title_fullStr | Harnessing the evolutionary information on oxygen binding proteins through Support Vector Machines based modules |
title_full_unstemmed | Harnessing the evolutionary information on oxygen binding proteins through Support Vector Machines based modules |
title_short | Harnessing the evolutionary information on oxygen binding proteins through Support Vector Machines based modules |
title_sort | harnessing the evolutionary information on oxygen binding proteins through support vector machines based modules |
topic | Research Note |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5948687/ https://www.ncbi.nlm.nih.gov/pubmed/29751818 http://dx.doi.org/10.1186/s13104-018-3383-9 |
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