Protein Secondary Structures Prediction based on Evolutionary Computation

In this paper we propose an approach based on evolutionary computation for the prediction of secondary protein structure motifs. The prediction model consists of a set of rules that predict both the beginning and the end of the regions corresponding to a secondary structure state conformation (α-hel...

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Autores: Márquez Chamorro, Alfonso Eduardo, Divina, Federico, Aguilar Ruiz, Jesús Salvador
Tipo de recurso: artículo
Estado:Versión enviada para evaluación y publicación
Fecha de publicación:2011
País:España
Institución:Universidad de Sevilla (US)
Repositorio:idUS. Depósito de Investigación de la Universidad de Sevilla
OAI Identifier:oai:idus.us.es:11441/133523
Acceso en línea:https://hdl.handle.net/11441/133523
https://doi.org/10.1145/2107756.2107758
Access Level:acceso abierto
Palabra clave:Protein secondary structure prediction
α-helix
β-strand
β-sheet
Evolutionary Computation
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spelling Protein Secondary Structures Prediction based on Evolutionary ComputationMárquez Chamorro, Alfonso EduardoDivina, FedericoAguilar Ruiz, Jesús SalvadorProtein secondary structure predictionα-helixβ-strandβ-sheetEvolutionary ComputationIn this paper we propose an approach based on evolutionary computation for the prediction of secondary protein structure motifs. The prediction model consists of a set of rules that predict both the beginning and the end of the regions corresponding to a secondary structure state conformation (α-helix or β-strand). The prediction is based on a set of specific amino acid physical chemical properties. In addition we also propose a statistical study regarding the propensities of each pair of amino acids in capping regions of α-helix and β-strand. Experimental results confirm the validity of our proposal.Association for Computing Machinery (ACM)Lenguajes y Sistemas InformáticosTIC205: Ingeniería del Software Aplicada2011info:eu-repo/semantics/articleinfo:eu-repo/semantics/submittedVersionapplication/pdfapplication/pdfhttps://hdl.handle.net/11441/133523https://doi.org/10.1145/2107756.2107758reponame:idUS. Depósito de Investigación de la Universidad de Sevillainstname:Universidad de Sevilla (US)InglésACM SIGAPP Applied Computing Review, 11 (4), 17-25.https://dl.acm.org/doi/10.1145/2107756.2107758info:eu-repo/semantics/openAccessoai:idus.us.es:11441/1335232026-06-17T12:51:07Z
dc.title.none.fl_str_mv Protein Secondary Structures Prediction based on Evolutionary Computation
title Protein Secondary Structures Prediction based on Evolutionary Computation
spellingShingle Protein Secondary Structures Prediction based on Evolutionary Computation
Márquez Chamorro, Alfonso Eduardo
Protein secondary structure prediction
α-helix
β-strand
β-sheet
Evolutionary Computation
title_short Protein Secondary Structures Prediction based on Evolutionary Computation
title_full Protein Secondary Structures Prediction based on Evolutionary Computation
title_fullStr Protein Secondary Structures Prediction based on Evolutionary Computation
title_full_unstemmed Protein Secondary Structures Prediction based on Evolutionary Computation
title_sort Protein Secondary Structures Prediction based on Evolutionary Computation
dc.creator.none.fl_str_mv Márquez Chamorro, Alfonso Eduardo
Divina, Federico
Aguilar Ruiz, Jesús Salvador
author Márquez Chamorro, Alfonso Eduardo
author_facet Márquez Chamorro, Alfonso Eduardo
Divina, Federico
Aguilar Ruiz, Jesús Salvador
author_role author
author2 Divina, Federico
Aguilar Ruiz, Jesús Salvador
author2_role author
author
dc.contributor.none.fl_str_mv Lenguajes y Sistemas Informáticos
TIC205: Ingeniería del Software Aplicada
dc.subject.none.fl_str_mv Protein secondary structure prediction
α-helix
β-strand
β-sheet
Evolutionary Computation
topic Protein secondary structure prediction
α-helix
β-strand
β-sheet
Evolutionary Computation
description In this paper we propose an approach based on evolutionary computation for the prediction of secondary protein structure motifs. The prediction model consists of a set of rules that predict both the beginning and the end of the regions corresponding to a secondary structure state conformation (α-helix or β-strand). The prediction is based on a set of specific amino acid physical chemical properties. In addition we also propose a statistical study regarding the propensities of each pair of amino acids in capping regions of α-helix and β-strand. Experimental results confirm the validity of our proposal.
publishDate 2011
dc.date.none.fl_str_mv 2011
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/submittedVersion
format article
status_str submittedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/11441/133523
https://doi.org/10.1145/2107756.2107758
url https://hdl.handle.net/11441/133523
https://doi.org/10.1145/2107756.2107758
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv ACM SIGAPP Applied Computing Review, 11 (4), 17-25.
https://dl.acm.org/doi/10.1145/2107756.2107758
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Association for Computing Machinery (ACM)
publisher.none.fl_str_mv Association for Computing Machinery (ACM)
dc.source.none.fl_str_mv reponame:idUS. Depósito de Investigación de la Universidad de Sevilla
instname:Universidad de Sevilla (US)
instname_str Universidad de Sevilla (US)
reponame_str idUS. Depósito de Investigación de la Universidad de Sevilla
collection idUS. Depósito de Investigación de la Universidad de Sevilla
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