Conformational diversity and the emergence of sequence signatures during evolution
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 behav...
| Autores: | , , , |
|---|---|
| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2015 |
| País: | Argentina |
| Institución: | Consejo Nacional de Investigaciones Científicas y Técnicas |
| Repositorio: | CONICET Digital (CONICET) |
| Idioma: | inglés |
| OAI Identifier: | oai:ri.conicet.gov.ar:11336/133664 |
| Acceso en línea: | http://hdl.handle.net/11336/133664 |
| Access Level: | acceso abierto |
| Palabra clave: | PROTEINS EVOLUTION CONFORMATIONAL DIVERSITY COEVOLUTION https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
| id |
AR_f010e85bf2d85a451fe8b74ba2dbe5e5 |
|---|---|
| oai_identifier_str |
oai:ri.conicet.gov.ar:11336/133664 |
| network_acronym_str |
AR |
| network_name_str |
Argentina |
| repository_id_str |
|
| 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 Técnicas2024-05-08T13:53:33Zoai: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:34982024-05-08 13:53:34.233CONICET 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 https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
| 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 https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
| topic |
PROTEINS EVOLUTION CONFORMATIONAL DIVERSITY COEVOLUTION https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
| 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 |
| instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
| reponame_str |
CONICET Digital (CONICET) |
| collection |
CONICET Digital (CONICET) |
| 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 |
| _version_ |
1799195472482533376 |
| score |
15,811543 |