Protein conformational diversity correlates with evolutionary rate

Autores
Zea, Diego Javier; Monzón, Alexander; Fornasari, Maria Silvina; Marino Buslje, Cristina; Parisi, Gustavo Daniel
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Native state of proteins is better represented by an ensemble of conformers in equilibrium than by only one structure. The extension of structural differences between conformers characterizes the conformational diversity of the protein. In this study, we found a negative correlation between conformational diversity and protein evolutionary rate. Conformational diversity was expressed as the maximum root mean square deviation (RMSD) between the available conformers in Conformational Diversity of Native State database. Evolutionary rate estimations were calculated using 16 different species compared with human sharing at least 700 orthologous proteins with known conformational diversity extension. The negative correlation found is independent of the protein expression level and comparable in magnitude and sign with the correlation between gene expression level and evolutionary rate. Our findings suggest that the structural constraints underlying protein dynamism, essential for protein function, could modulate protein divergence.
Fil: Zea, Diego Javier. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Monzón, Alexander. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Fornasari, Maria Silvina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Marino Buslje, Cristina. Fundación Instituto Leloir; Argentina
Fil: Parisi, Gustavo Daniel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
Evolutionary Rate
Protein Evolution
Conformational Diversity
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/23895
Acceder
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spelling Protein conformational diversity correlates with evolutionary rateZea, Diego JavierMonzón, AlexanderFornasari, Maria SilvinaMarino Buslje, CristinaParisi, Gustavo DanielEvolutionary RateProtein EvolutionConformational Diversityhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Native state of proteins is better represented by an ensemble of conformers in equilibrium than by only one structure. The extension of structural differences between conformers characterizes the conformational diversity of the protein. In this study, we found a negative correlation between conformational diversity and protein evolutionary rate. Conformational diversity was expressed as the maximum root mean square deviation (RMSD) between the available conformers in Conformational Diversity of Native State database. Evolutionary rate estimations were calculated using 16 different species compared with human sharing at least 700 orthologous proteins with known conformational diversity extension. The negative correlation found is independent of the protein expression level and comparable in magnitude and sign with the correlation between gene expression level and evolutionary rate. Our findings suggest that the structural constraints underlying protein dynamism, essential for protein function, could modulate protein divergence.Fil: Zea, Diego Javier. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Monzón, Alexander. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Fornasari, Maria Silvina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Marino Buslje, Cristina. Fundación Instituto Leloir; ArgentinaFil: Parisi, Gustavo Daniel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaOxford University Press2013-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/23895Zea, Diego Javier; Monzón, Alexander; Fornasari, Maria Silvina; Marino Buslje, Cristina; Parisi, Gustavo Daniel; Protein conformational diversity correlates with evolutionary rate; Oxford University Press; Molecular Biology and Evolution; 30; 7; 4-2013; 1500-15030737-4038CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1093/molbev/mst065info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/mbe/article-lookup/doi/10.1093/molbev/mst065info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-17T10:50:11Zoai:ri.conicet.gov.ar:11336/23895instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-17 10:50:11.91CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Protein conformational diversity correlates with evolutionary rate
title Protein conformational diversity correlates with evolutionary rate
spellingShingle Protein conformational diversity correlates with evolutionary rate
Zea, Diego Javier
Evolutionary Rate
Protein Evolution
Conformational Diversity
title_short Protein conformational diversity correlates with evolutionary rate
title_full Protein conformational diversity correlates with evolutionary rate
title_fullStr Protein conformational diversity correlates with evolutionary rate
title_full_unstemmed Protein conformational diversity correlates with evolutionary rate
title_sort Protein conformational diversity correlates with evolutionary rate
dc.creator.none.fl_str_mv Zea, Diego Javier
Monzón, Alexander
Fornasari, Maria Silvina
Marino Buslje, Cristina
Parisi, Gustavo Daniel
author Zea, Diego Javier
author_facet Zea, Diego Javier
Monzón, Alexander
Fornasari, Maria Silvina
Marino Buslje, Cristina
Parisi, Gustavo Daniel
author_role author
author2 Monzón, Alexander
Fornasari, Maria Silvina
Marino Buslje, Cristina
Parisi, Gustavo Daniel
author2_role author
author
author
author
dc.subject.none.fl_str_mv Evolutionary Rate
Protein Evolution
Conformational Diversity
topic Evolutionary Rate
Protein Evolution
Conformational Diversity
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Native state of proteins is better represented by an ensemble of conformers in equilibrium than by only one structure. The extension of structural differences between conformers characterizes the conformational diversity of the protein. In this study, we found a negative correlation between conformational diversity and protein evolutionary rate. Conformational diversity was expressed as the maximum root mean square deviation (RMSD) between the available conformers in Conformational Diversity of Native State database. Evolutionary rate estimations were calculated using 16 different species compared with human sharing at least 700 orthologous proteins with known conformational diversity extension. The negative correlation found is independent of the protein expression level and comparable in magnitude and sign with the correlation between gene expression level and evolutionary rate. Our findings suggest that the structural constraints underlying protein dynamism, essential for protein function, could modulate protein divergence.
Fil: Zea, Diego Javier. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Monzón, Alexander. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Fornasari, Maria Silvina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Marino Buslje, Cristina. Fundación Instituto Leloir; Argentina
Fil: Parisi, Gustavo Daniel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description Native state of proteins is better represented by an ensemble of conformers in equilibrium than by only one structure. The extension of structural differences between conformers characterizes the conformational diversity of the protein. In this study, we found a negative correlation between conformational diversity and protein evolutionary rate. Conformational diversity was expressed as the maximum root mean square deviation (RMSD) between the available conformers in Conformational Diversity of Native State database. Evolutionary rate estimations were calculated using 16 different species compared with human sharing at least 700 orthologous proteins with known conformational diversity extension. The negative correlation found is independent of the protein expression level and comparable in magnitude and sign with the correlation between gene expression level and evolutionary rate. Our findings suggest that the structural constraints underlying protein dynamism, essential for protein function, could modulate protein divergence.
publishDate 2013
dc.date.none.fl_str_mv 2013-04
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/23895
Zea, Diego Javier; Monzón, Alexander; Fornasari, Maria Silvina; Marino Buslje, Cristina; Parisi, Gustavo Daniel; Protein conformational diversity correlates with evolutionary rate; Oxford University Press; Molecular Biology and Evolution; 30; 7; 4-2013; 1500-1503
0737-4038
CONICET Digital
CONICET
url http://hdl.handle.net/11336/23895
identifier_str_mv Zea, Diego Javier; Monzón, Alexander; Fornasari, Maria Silvina; Marino Buslje, Cristina; Parisi, Gustavo Daniel; Protein conformational diversity correlates with evolutionary rate; Oxford University Press; Molecular Biology and Evolution; 30; 7; 4-2013; 1500-1503
0737-4038
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1093/molbev/mst065
info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/mbe/article-lookup/doi/10.1093/molbev/mst065
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Oxford University Press
publisher.none.fl_str_mv Oxford University Press
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.001348

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