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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/263037
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling 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 Técnicas2025-10-22T12:12:05Zoai: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:34982025-10-22 12:12:06.052CONICET 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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score 12.982451

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