Frustraevo: a web server to localize and quantify the conservation of local energetic frustration in protein families
- Autores
- Parra, Rodrigo Gonzalo; Freiberger, Maria Ines; Poley Gil, Miriam; Fernandez Martin, Miguel; Radusky, Leandro Gabriel; Ruiz Serra, Victoria; Wolynes, Peter G.; Ferreiro, Diego; Valencia, Alfonso
- Año de publicación
- 2024
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- According to the Principle of Minimal Frustration, folded proteins can only have a minimal number of strong energetic conflicts in their native states. However, not all interactions are energetically optimized for folding but some remain in energetic conflict, i.e. they are highly frustrated. This remaining local energetic frustration has been shown to be statistically correlated with distinct functional aspects such as protein-protein interaction sites, allosterism and catalysis. Fuelled by the recent breakthroughs in efficient protein structure prediction that have made available good quality models for most proteins, we have developed a strategy to calculate local energetic frustration within large protein families and quantify its conservation over evolutionary time. Based on this evolutionary information we can identify how stability and functional constraints have appeared at the common ancestor of the family and have been maintained over the course of evolution. Here, we present FrustraEvo, a web server tool to calculate and quantify the conservation of local energetic frustration in protein families.
Fil: Parra, Rodrigo Gonzalo. Barcelona Supercomputing Center; España
Fil: Freiberger, Maria Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica. Laboratorio de Fisiología de Proteínas; Argentina
Fil: Poley Gil, Miriam. Barcelona Supercomputing Center; España
Fil: Fernandez Martin, Miguel. Barcelona Supercomputing Center; España
Fil: Radusky, Leandro Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Ruiz Serra, Victoria. Barcelona Supercomputing Center; España
Fil: Wolynes, Peter G.. Rice University; Estados Unidos
Fil: Ferreiro, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica. Laboratorio de Fisiología de Proteínas; Argentina
Fil: Valencia, Alfonso. Barcelona Supercomputing Center; España. Institució Catalana de Recerca i Estudis Avancats; España - Materia
-
Protein evolution
Local frustration - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/265246
Ver los metadatos del registro completo
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Frustraevo: a web server to localize and quantify the conservation of local energetic frustration in protein familiesParra, Rodrigo GonzaloFreiberger, Maria InesPoley Gil, MiriamFernandez Martin, MiguelRadusky, Leandro GabrielRuiz Serra, VictoriaWolynes, Peter G.Ferreiro, DiegoValencia, AlfonsoProtein evolutionLocal frustrationhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1According to the Principle of Minimal Frustration, folded proteins can only have a minimal number of strong energetic conflicts in their native states. However, not all interactions are energetically optimized for folding but some remain in energetic conflict, i.e. they are highly frustrated. This remaining local energetic frustration has been shown to be statistically correlated with distinct functional aspects such as protein-protein interaction sites, allosterism and catalysis. Fuelled by the recent breakthroughs in efficient protein structure prediction that have made available good quality models for most proteins, we have developed a strategy to calculate local energetic frustration within large protein families and quantify its conservation over evolutionary time. Based on this evolutionary information we can identify how stability and functional constraints have appeared at the common ancestor of the family and have been maintained over the course of evolution. Here, we present FrustraEvo, a web server tool to calculate and quantify the conservation of local energetic frustration in protein families.Fil: Parra, Rodrigo Gonzalo. Barcelona Supercomputing Center; EspañaFil: Freiberger, Maria Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica. Laboratorio de Fisiología de Proteínas; ArgentinaFil: Poley Gil, Miriam. Barcelona Supercomputing Center; EspañaFil: Fernandez Martin, Miguel. Barcelona Supercomputing Center; EspañaFil: Radusky, Leandro Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Ruiz Serra, Victoria. Barcelona Supercomputing Center; EspañaFil: Wolynes, Peter G.. Rice University; Estados UnidosFil: Ferreiro, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica. Laboratorio de Fisiología de Proteínas; ArgentinaFil: Valencia, Alfonso. Barcelona Supercomputing Center; España. Institució Catalana de Recerca i Estudis Avancats; EspañaOxford University Press2024-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/265246Parra, Rodrigo Gonzalo; Freiberger, Maria Ines; Poley Gil, Miriam; Fernandez Martin, Miguel; Radusky, Leandro Gabriel; et al.; Frustraevo: a web server to localize and quantify the conservation of local energetic frustration in protein families; Oxford University Press; Nucleic Acids Research; 52; W1; 7-2024; W233-W2370305-10481362-4962CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/nar/advance-article/doi/10.1093/nar/gkae244/7642057info:eu-repo/semantics/altIdentifier/doi/10.1093/nar/gkae244info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:20:37Zoai:ri.conicet.gov.ar:11336/265246instacron: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:34982025-09-29 10:20:37.333CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Frustraevo: a web server to localize and quantify the conservation of local energetic frustration in protein families |
title |
Frustraevo: a web server to localize and quantify the conservation of local energetic frustration in protein families |
spellingShingle |
Frustraevo: a web server to localize and quantify the conservation of local energetic frustration in protein families Parra, Rodrigo Gonzalo Protein evolution Local frustration |
title_short |
Frustraevo: a web server to localize and quantify the conservation of local energetic frustration in protein families |
title_full |
Frustraevo: a web server to localize and quantify the conservation of local energetic frustration in protein families |
title_fullStr |
Frustraevo: a web server to localize and quantify the conservation of local energetic frustration in protein families |
title_full_unstemmed |
Frustraevo: a web server to localize and quantify the conservation of local energetic frustration in protein families |
title_sort |
Frustraevo: a web server to localize and quantify the conservation of local energetic frustration in protein families |
dc.creator.none.fl_str_mv |
Parra, Rodrigo Gonzalo Freiberger, Maria Ines Poley Gil, Miriam Fernandez Martin, Miguel Radusky, Leandro Gabriel Ruiz Serra, Victoria Wolynes, Peter G. Ferreiro, Diego Valencia, Alfonso |
author |
Parra, Rodrigo Gonzalo |
author_facet |
Parra, Rodrigo Gonzalo Freiberger, Maria Ines Poley Gil, Miriam Fernandez Martin, Miguel Radusky, Leandro Gabriel Ruiz Serra, Victoria Wolynes, Peter G. Ferreiro, Diego Valencia, Alfonso |
author_role |
author |
author2 |
Freiberger, Maria Ines Poley Gil, Miriam Fernandez Martin, Miguel Radusky, Leandro Gabriel Ruiz Serra, Victoria Wolynes, Peter G. Ferreiro, Diego Valencia, Alfonso |
author2_role |
author author author author author author author author |
dc.subject.none.fl_str_mv |
Protein evolution Local frustration |
topic |
Protein evolution Local frustration |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
According to the Principle of Minimal Frustration, folded proteins can only have a minimal number of strong energetic conflicts in their native states. However, not all interactions are energetically optimized for folding but some remain in energetic conflict, i.e. they are highly frustrated. This remaining local energetic frustration has been shown to be statistically correlated with distinct functional aspects such as protein-protein interaction sites, allosterism and catalysis. Fuelled by the recent breakthroughs in efficient protein structure prediction that have made available good quality models for most proteins, we have developed a strategy to calculate local energetic frustration within large protein families and quantify its conservation over evolutionary time. Based on this evolutionary information we can identify how stability and functional constraints have appeared at the common ancestor of the family and have been maintained over the course of evolution. Here, we present FrustraEvo, a web server tool to calculate and quantify the conservation of local energetic frustration in protein families. Fil: Parra, Rodrigo Gonzalo. Barcelona Supercomputing Center; España Fil: Freiberger, Maria Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica. Laboratorio de Fisiología de Proteínas; Argentina Fil: Poley Gil, Miriam. Barcelona Supercomputing Center; España Fil: Fernandez Martin, Miguel. Barcelona Supercomputing Center; España Fil: Radusky, Leandro Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Ruiz Serra, Victoria. Barcelona Supercomputing Center; España Fil: Wolynes, Peter G.. Rice University; Estados Unidos Fil: Ferreiro, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica. Laboratorio de Fisiología de Proteínas; Argentina Fil: Valencia, Alfonso. Barcelona Supercomputing Center; España. Institució Catalana de Recerca i Estudis Avancats; España |
description |
According to the Principle of Minimal Frustration, folded proteins can only have a minimal number of strong energetic conflicts in their native states. However, not all interactions are energetically optimized for folding but some remain in energetic conflict, i.e. they are highly frustrated. This remaining local energetic frustration has been shown to be statistically correlated with distinct functional aspects such as protein-protein interaction sites, allosterism and catalysis. Fuelled by the recent breakthroughs in efficient protein structure prediction that have made available good quality models for most proteins, we have developed a strategy to calculate local energetic frustration within large protein families and quantify its conservation over evolutionary time. Based on this evolutionary information we can identify how stability and functional constraints have appeared at the common ancestor of the family and have been maintained over the course of evolution. Here, we present FrustraEvo, a web server tool to calculate and quantify the conservation of local energetic frustration in protein families. |
publishDate |
2024 |
dc.date.none.fl_str_mv |
2024-07 |
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/11336/265246 Parra, Rodrigo Gonzalo; Freiberger, Maria Ines; Poley Gil, Miriam; Fernandez Martin, Miguel; Radusky, Leandro Gabriel; et al.; Frustraevo: a web server to localize and quantify the conservation of local energetic frustration in protein families; Oxford University Press; Nucleic Acids Research; 52; W1; 7-2024; W233-W237 0305-1048 1362-4962 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/265246 |
identifier_str_mv |
Parra, Rodrigo Gonzalo; Freiberger, Maria Ines; Poley Gil, Miriam; Fernandez Martin, Miguel; Radusky, Leandro Gabriel; et al.; Frustraevo: a web server to localize and quantify the conservation of local energetic frustration in protein families; Oxford University Press; Nucleic Acids Research; 52; W1; 7-2024; W233-W237 0305-1048 1362-4962 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/nar/advance-article/doi/10.1093/nar/gkae244/7642057 info:eu-repo/semantics/altIdentifier/doi/10.1093/nar/gkae244 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc/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 |
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CONICET Digital (CONICET) |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
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dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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13.070432 |