Frustration, function and folding
- Autores
- Ferreiro, Diego; Komives, Elizabeth A.; Wolynes, Peter G.
- Año de publicación
- 2018
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Natural protein molecules are exceptional polymers. Encoded in apparently random strings of amino-acids, these objects perform clear physical tasks that are rare to find by simple chance. Accurate folding, specific binding, powerful catalysis, are examples of basic chemical activities that the great majority of polypeptides do not display, and are thought to be the outcome of the natural history of proteins. Function, a concept genuine to Biology, is at the core of evolution and often conflicts with the physical constraints. Locating the frustration between discrepant goals in a recurrent system leads to fundamental insights about the chances and necessities that shape the encoding of biological information.
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
Fil: Komives, Elizabeth A.. University of California at San Diego; Estados Unidos
Fil: Wolynes, Peter G.. Rice University; Estados Unidos - Materia
-
Protein folding
Protein function - 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:11336/93870
Ver los metadatos del registro completo
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Frustration, function and foldingFerreiro, DiegoKomives, Elizabeth A.Wolynes, Peter G.Protein foldingProtein functionhttps://purl.org/becyt/ford/1.7https://purl.org/becyt/ford/1Natural protein molecules are exceptional polymers. Encoded in apparently random strings of amino-acids, these objects perform clear physical tasks that are rare to find by simple chance. Accurate folding, specific binding, powerful catalysis, are examples of basic chemical activities that the great majority of polypeptides do not display, and are thought to be the outcome of the natural history of proteins. Function, a concept genuine to Biology, is at the core of evolution and often conflicts with the physical constraints. Locating the frustration between discrepant goals in a recurrent system leads to fundamental insights about the chances and necessities that shape the encoding of biological information.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; ArgentinaFil: Komives, Elizabeth A.. University of California at San Diego; Estados UnidosFil: Wolynes, Peter G.. Rice University; Estados UnidosCurrent Biology2018-02-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/93870Ferreiro, Diego; Komives, Elizabeth A.; Wolynes, Peter G.; Frustration, function and folding; Current Biology; Current Opinion In Structural Biology; 48; 5-2-2018; 68-730959-440XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.sbi.2017.09.006info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0959440X17300726info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6005193/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:39:59Zoai:ri.conicet.gov.ar:11336/93870instacron: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 10:39:59.58CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Frustration, function and folding |
title |
Frustration, function and folding |
spellingShingle |
Frustration, function and folding Ferreiro, Diego Protein folding Protein function |
title_short |
Frustration, function and folding |
title_full |
Frustration, function and folding |
title_fullStr |
Frustration, function and folding |
title_full_unstemmed |
Frustration, function and folding |
title_sort |
Frustration, function and folding |
dc.creator.none.fl_str_mv |
Ferreiro, Diego Komives, Elizabeth A. Wolynes, Peter G. |
author |
Ferreiro, Diego |
author_facet |
Ferreiro, Diego Komives, Elizabeth A. Wolynes, Peter G. |
author_role |
author |
author2 |
Komives, Elizabeth A. Wolynes, Peter G. |
author2_role |
author author |
dc.subject.none.fl_str_mv |
Protein folding Protein function |
topic |
Protein folding Protein function |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.7 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Natural protein molecules are exceptional polymers. Encoded in apparently random strings of amino-acids, these objects perform clear physical tasks that are rare to find by simple chance. Accurate folding, specific binding, powerful catalysis, are examples of basic chemical activities that the great majority of polypeptides do not display, and are thought to be the outcome of the natural history of proteins. Function, a concept genuine to Biology, is at the core of evolution and often conflicts with the physical constraints. Locating the frustration between discrepant goals in a recurrent system leads to fundamental insights about the chances and necessities that shape the encoding of biological information. 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 Fil: Komives, Elizabeth A.. University of California at San Diego; Estados Unidos Fil: Wolynes, Peter G.. Rice University; Estados Unidos |
description |
Natural protein molecules are exceptional polymers. Encoded in apparently random strings of amino-acids, these objects perform clear physical tasks that are rare to find by simple chance. Accurate folding, specific binding, powerful catalysis, are examples of basic chemical activities that the great majority of polypeptides do not display, and are thought to be the outcome of the natural history of proteins. Function, a concept genuine to Biology, is at the core of evolution and often conflicts with the physical constraints. Locating the frustration between discrepant goals in a recurrent system leads to fundamental insights about the chances and necessities that shape the encoding of biological information. |
publishDate |
2018 |
dc.date.none.fl_str_mv |
2018-02-05 |
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/11336/93870 Ferreiro, Diego; Komives, Elizabeth A.; Wolynes, Peter G.; Frustration, function and folding; Current Biology; Current Opinion In Structural Biology; 48; 5-2-2018; 68-73 0959-440X CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/93870 |
identifier_str_mv |
Ferreiro, Diego; Komives, Elizabeth A.; Wolynes, Peter G.; Frustration, function and folding; Current Biology; Current Opinion In Structural Biology; 48; 5-2-2018; 68-73 0959-440X CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.sbi.2017.09.006 info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0959440X17300726 info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6005193/ |
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 |
dc.publisher.none.fl_str_mv |
Current Biology |
publisher.none.fl_str_mv |
Current Biology |
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reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
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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 |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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13.070432 |