Conformational diversity and the emergence of sequence signatures during evolution

Autores
Parisi, Gustavo Daniel; Zea, Diego Javier; Monzón, Alexander; Marino Buslje, Cristina
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Proteins' native structure is an ensemble of conformers in equilibrium, including all their respective functional states and intermediates. The induced-fit first and the pre-equilibrium theories later, described how structural changes are required to explain the allosteric and cooperative behaviours in proteins, which are key to protein function. The conformational ensemble concept has become a key tool in explaining an endless list of essential protein properties such as function, enzyme and antibody promiscuity, signal transduction, protein-protein recognition, origin of diseases, origin of new protein functions, evolutionary rate and order-disorder transitions, among others. Conformational diversity is encoded by the amino acid sequence and such a signature can be evidenced through evolutionary studies as evolutionary rate, conservation and coevolution.
Fil: Parisi, Gustavo Daniel. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Zea, Diego Javier. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Monzón, Alexander. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Marino Buslje, Cristina. Fundación Instituto Leloir; Argentina
Materia
PROTEINS
EVOLUTION
CONFORMATIONAL DIVERSITY
COEVOLUTION
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:11336/133664
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Conformational diversity and the emergence of sequence signatures during evolutionParisi, Gustavo DanielZea, Diego JavierMonzón, AlexanderMarino Buslje, CristinaPROTEINSEVOLUTIONCONFORMATIONAL DIVERSITYCOEVOLUTIONhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Proteins' native structure is an ensemble of conformers in equilibrium, including all their respective functional states and intermediates. The induced-fit first and the pre-equilibrium theories later, described how structural changes are required to explain the allosteric and cooperative behaviours in proteins, which are key to protein function. The conformational ensemble concept has become a key tool in explaining an endless list of essential protein properties such as function, enzyme and antibody promiscuity, signal transduction, protein-protein recognition, origin of diseases, origin of new protein functions, evolutionary rate and order-disorder transitions, among others. Conformational diversity is encoded by the amino acid sequence and such a signature can be evidenced through evolutionary studies as evolutionary rate, conservation and coevolution.Fil: Parisi, Gustavo Daniel. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Zea, Diego Javier. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Monzón, Alexander. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Marino Buslje, Cristina. Fundación Instituto Leloir; ArgentinaCurrent Biology2015-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/133664Parisi, Gustavo Daniel; Zea, Diego Javier; Monzón, Alexander; Marino Buslje, Cristina; Conformational diversity and the emergence of sequence signatures during evolution; Current Biology; Current Opinion In Structural Biology; 32; 3-2015; 58-650959-440X1879-033XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0959440X15000147info:eu-repo/semantics/altIdentifier/doi/10.1016/j.sbi.2015.02.005info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:59:43Zoai:ri.conicet.gov.ar:11336/133664instacron: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 09:59:43.612CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Conformational diversity and the emergence of sequence signatures during evolution
title Conformational diversity and the emergence of sequence signatures during evolution
spellingShingle Conformational diversity and the emergence of sequence signatures during evolution
Parisi, Gustavo Daniel
PROTEINS
EVOLUTION
CONFORMATIONAL DIVERSITY
COEVOLUTION
title_short Conformational diversity and the emergence of sequence signatures during evolution
title_full Conformational diversity and the emergence of sequence signatures during evolution
title_fullStr Conformational diversity and the emergence of sequence signatures during evolution
title_full_unstemmed Conformational diversity and the emergence of sequence signatures during evolution
title_sort Conformational diversity and the emergence of sequence signatures during evolution
dc.creator.none.fl_str_mv Parisi, Gustavo Daniel
Zea, Diego Javier
Monzón, Alexander
Marino Buslje, Cristina
author Parisi, Gustavo Daniel
author_facet Parisi, Gustavo Daniel
Zea, Diego Javier
Monzón, Alexander
Marino Buslje, Cristina
author_role author
author2 Zea, Diego Javier
Monzón, Alexander
Marino Buslje, Cristina
author2_role author
author
author
dc.subject.none.fl_str_mv PROTEINS
EVOLUTION
CONFORMATIONAL DIVERSITY
COEVOLUTION
topic PROTEINS
EVOLUTION
CONFORMATIONAL DIVERSITY
COEVOLUTION
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Proteins' native structure is an ensemble of conformers in equilibrium, including all their respective functional states and intermediates. The induced-fit first and the pre-equilibrium theories later, described how structural changes are required to explain the allosteric and cooperative behaviours in proteins, which are key to protein function. The conformational ensemble concept has become a key tool in explaining an endless list of essential protein properties such as function, enzyme and antibody promiscuity, signal transduction, protein-protein recognition, origin of diseases, origin of new protein functions, evolutionary rate and order-disorder transitions, among others. Conformational diversity is encoded by the amino acid sequence and such a signature can be evidenced through evolutionary studies as evolutionary rate, conservation and coevolution.
Fil: Parisi, Gustavo Daniel. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Zea, Diego Javier. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Monzón, Alexander. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Marino Buslje, Cristina. Fundación Instituto Leloir; Argentina
description Proteins' native structure is an ensemble of conformers in equilibrium, including all their respective functional states and intermediates. The induced-fit first and the pre-equilibrium theories later, described how structural changes are required to explain the allosteric and cooperative behaviours in proteins, which are key to protein function. The conformational ensemble concept has become a key tool in explaining an endless list of essential protein properties such as function, enzyme and antibody promiscuity, signal transduction, protein-protein recognition, origin of diseases, origin of new protein functions, evolutionary rate and order-disorder transitions, among others. Conformational diversity is encoded by the amino acid sequence and such a signature can be evidenced through evolutionary studies as evolutionary rate, conservation and coevolution.
publishDate 2015
dc.date.none.fl_str_mv 2015-03
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/11336/133664
Parisi, Gustavo Daniel; Zea, Diego Javier; Monzón, Alexander; Marino Buslje, Cristina; Conformational diversity and the emergence of sequence signatures during evolution; Current Biology; Current Opinion In Structural Biology; 32; 3-2015; 58-65
0959-440X
1879-033X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/133664
identifier_str_mv Parisi, Gustavo Daniel; Zea, Diego Javier; Monzón, Alexander; Marino Buslje, Cristina; Conformational diversity and the emergence of sequence signatures during evolution; Current Biology; Current Opinion In Structural Biology; 32; 3-2015; 58-65
0959-440X
1879-033X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0959440X15000147
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.sbi.2015.02.005
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
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Current Biology
publisher.none.fl_str_mv Current Biology
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 13.070432

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