Reassessing the Exon-Foldon correspondence using Frustration Analysis
- Autores
- Galpern, Ezequiel Alejandro; Jaafari, Hana; Bueno, Carlos; Wolynes, Peter G.; Ferreiro, Diego
- Año de publicación
- 2024
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Protein folding and evolution are intimately linked phenomena. Here, we revisit the concept of exons as potential protein folding modules across 38 abundant and conserved protein families. Taking advantage of genomic exon-intron organization and extensive protein sequence data, we explore exon boundary conservation and assess their foldon-like behavior using energy landscape theoretic measurements. We found deviations in exon size distribution from exponential decay indicating selection in evolution. We describe that there is a pronounced independent foldability of segments corresponding to conserved exons, supporting the exon-foldon correspondence. We further develop a systematic partitioning of protein domains using exon boundary hot spots, unveiling minimal common exons consisting of uninterrupted alpha and/or beta elements for the majority but not all of the studied families.
Fil: Galpern, Ezequiel Alejandro. 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; Argentina
Fil: Jaafari, Hana. Rice University; Estados Unidos
Fil: Bueno, Carlos. Rice University; Estados Unidos
Fil: Wolynes, Peter G.. Rice University; Estados Unidos
Fil: Ferreiro, Diego. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. 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 - Materia
-
EXON
PROTEIN FOLDING
ENERGY LANDSCAPE
FOLDON - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/263037
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Reassessing the Exon-Foldon correspondence using Frustration AnalysisGalpern, Ezequiel AlejandroJaafari, HanaBueno, CarlosWolynes, Peter G.Ferreiro, DiegoEXONPROTEIN FOLDINGENERGY LANDSCAPEFOLDONhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Protein folding and evolution are intimately linked phenomena. Here, we revisit the concept of exons as potential protein folding modules across 38 abundant and conserved protein families. Taking advantage of genomic exon-intron organization and extensive protein sequence data, we explore exon boundary conservation and assess their foldon-like behavior using energy landscape theoretic measurements. We found deviations in exon size distribution from exponential decay indicating selection in evolution. We describe that there is a pronounced independent foldability of segments corresponding to conserved exons, supporting the exon-foldon correspondence. We further develop a systematic partitioning of protein domains using exon boundary hot spots, unveiling minimal common exons consisting of uninterrupted alpha and/or beta elements for the majority but not all of the studied families.Fil: Galpern, Ezequiel Alejandro. 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; ArgentinaFil: Jaafari, Hana. Rice University; Estados UnidosFil: Bueno, Carlos. Rice University; Estados UnidosFil: Wolynes, Peter G.. Rice University; Estados UnidosFil: Ferreiro, Diego. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. 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; ArgentinaCornell University2024-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/263037Galpern, Ezequiel Alejandro; Jaafari, Hana; Bueno, Carlos; Wolynes, Peter G.; Ferreiro, Diego; Reassessing the Exon-Foldon correspondence using Frustration Analysis; Cornell University; ArXiv.org; 1-2024; 1-182331-8422CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/arxiv/https://arxiv.org/abs/2401.02371info:eu-repo/semantics/altIdentifier/doi/10.48550/arXiv.2401.02371info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:39:45Zoai:ri.conicet.gov.ar:11336/263037instacron: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 10:39:45.771CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Reassessing the Exon-Foldon correspondence using Frustration Analysis |
title |
Reassessing the Exon-Foldon correspondence using Frustration Analysis |
spellingShingle |
Reassessing the Exon-Foldon correspondence using Frustration Analysis Galpern, Ezequiel Alejandro EXON PROTEIN FOLDING ENERGY LANDSCAPE FOLDON |
title_short |
Reassessing the Exon-Foldon correspondence using Frustration Analysis |
title_full |
Reassessing the Exon-Foldon correspondence using Frustration Analysis |
title_fullStr |
Reassessing the Exon-Foldon correspondence using Frustration Analysis |
title_full_unstemmed |
Reassessing the Exon-Foldon correspondence using Frustration Analysis |
title_sort |
Reassessing the Exon-Foldon correspondence using Frustration Analysis |
dc.creator.none.fl_str_mv |
Galpern, Ezequiel Alejandro Jaafari, Hana Bueno, Carlos Wolynes, Peter G. Ferreiro, Diego |
author |
Galpern, Ezequiel Alejandro |
author_facet |
Galpern, Ezequiel Alejandro Jaafari, Hana Bueno, Carlos Wolynes, Peter G. Ferreiro, Diego |
author_role |
author |
author2 |
Jaafari, Hana Bueno, Carlos Wolynes, Peter G. Ferreiro, Diego |
author2_role |
author author author author |
dc.subject.none.fl_str_mv |
EXON PROTEIN FOLDING ENERGY LANDSCAPE FOLDON |
topic |
EXON PROTEIN FOLDING ENERGY LANDSCAPE FOLDON |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Protein folding and evolution are intimately linked phenomena. Here, we revisit the concept of exons as potential protein folding modules across 38 abundant and conserved protein families. Taking advantage of genomic exon-intron organization and extensive protein sequence data, we explore exon boundary conservation and assess their foldon-like behavior using energy landscape theoretic measurements. We found deviations in exon size distribution from exponential decay indicating selection in evolution. We describe that there is a pronounced independent foldability of segments corresponding to conserved exons, supporting the exon-foldon correspondence. We further develop a systematic partitioning of protein domains using exon boundary hot spots, unveiling minimal common exons consisting of uninterrupted alpha and/or beta elements for the majority but not all of the studied families. Fil: Galpern, Ezequiel Alejandro. 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; Argentina Fil: Jaafari, Hana. Rice University; Estados Unidos Fil: Bueno, Carlos. Rice University; Estados Unidos Fil: Wolynes, Peter G.. Rice University; Estados Unidos Fil: Ferreiro, Diego. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. 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 |
description |
Protein folding and evolution are intimately linked phenomena. Here, we revisit the concept of exons as potential protein folding modules across 38 abundant and conserved protein families. Taking advantage of genomic exon-intron organization and extensive protein sequence data, we explore exon boundary conservation and assess their foldon-like behavior using energy landscape theoretic measurements. We found deviations in exon size distribution from exponential decay indicating selection in evolution. We describe that there is a pronounced independent foldability of segments corresponding to conserved exons, supporting the exon-foldon correspondence. We further develop a systematic partitioning of protein domains using exon boundary hot spots, unveiling minimal common exons consisting of uninterrupted alpha and/or beta elements for the majority but not all of the studied families. |
publishDate |
2024 |
dc.date.none.fl_str_mv |
2024-01 |
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/11336/263037 Galpern, Ezequiel Alejandro; Jaafari, Hana; Bueno, Carlos; Wolynes, Peter G.; Ferreiro, Diego; Reassessing the Exon-Foldon correspondence using Frustration Analysis; Cornell University; ArXiv.org; 1-2024; 1-18 2331-8422 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/263037 |
identifier_str_mv |
Galpern, Ezequiel Alejandro; Jaafari, Hana; Bueno, Carlos; Wolynes, Peter G.; Ferreiro, Diego; Reassessing the Exon-Foldon correspondence using Frustration Analysis; Cornell University; ArXiv.org; 1-2024; 1-18 2331-8422 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/arxiv/https://arxiv.org/abs/2401.02371 info:eu-repo/semantics/altIdentifier/doi/10.48550/arXiv.2401.02371 |
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 |
Cornell University |
publisher.none.fl_str_mv |
Cornell University |
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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1844614423679860736 |
score |
13.070432 |