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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...

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Autores principales: Muthukrishnan, Selvaraj, Puri, Munish
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2018
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.
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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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