On the role of frustration in the energy landscapes of allosteric proteins
- Autores
- Ferreiro, Diego; Hegler, Joseph A.; Komives, Elizabeth A.; Wolynes, Peter G.
- Año de publicación
- 2011
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Natural protein domains must be sufficiently stable to fold but often need to be locally unstable to function. Overall, strong energetic conflicts are minimized in native states satisfying the principle of minimal frustration. Local violations of this principle open up possibilities to form the complex multifunnel energy landscapes needed for large-scale conformational changes. We survey the local frustration patterns of allosteric domains and show that the regions that reconfigure are often enriched in patches of highly frustrated interactions, consistent both with the idea that these locally frustrated regions may act as specific hinges or that proteins may "crack" in these locations. On the other hand, the symmetry of multimeric protein assemblies allows near degeneracy by reconfiguring while maintaining minimally frustrated interactions. We also anecdotally examine some specific examples of complex conformational changes and speculate on the role of frustration in the kinetics of allosteric change.
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; Argentina
Fil: Hegler, Joseph A.. University of California at San Diego; Estados Unidos
Fil: Komives, Elizabeth A.. University of California at San Diego; Estados Unidos
Fil: Wolynes, Peter G.. University of California at San Diego; Estados Unidos - Materia
-
Minimal Frustration Principle
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:11336/68870
Ver los metadatos del registro completo
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On the role of frustration in the energy landscapes of allosteric proteinsFerreiro, DiegoHegler, Joseph A.Komives, Elizabeth A.Wolynes, Peter G.Minimal Frustration PrincipleProtein FoldingProtein Functionhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Natural protein domains must be sufficiently stable to fold but often need to be locally unstable to function. Overall, strong energetic conflicts are minimized in native states satisfying the principle of minimal frustration. Local violations of this principle open up possibilities to form the complex multifunnel energy landscapes needed for large-scale conformational changes. We survey the local frustration patterns of allosteric domains and show that the regions that reconfigure are often enriched in patches of highly frustrated interactions, consistent both with the idea that these locally frustrated regions may act as specific hinges or that proteins may "crack" in these locations. On the other hand, the symmetry of multimeric protein assemblies allows near degeneracy by reconfiguring while maintaining minimally frustrated interactions. We also anecdotally examine some specific examples of complex conformational changes and speculate on the role of frustration in the kinetics of allosteric change.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; ArgentinaFil: Hegler, Joseph A.. University of California at San Diego; Estados UnidosFil: Komives, Elizabeth A.. University of California at San Diego; Estados UnidosFil: Wolynes, Peter G.. University of California at San Diego; Estados UnidosNational Academy of Sciences2011-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/68870Ferreiro, Diego; Hegler, Joseph A.; Komives, Elizabeth A.; Wolynes, Peter G.; On the role of frustration in the energy landscapes of allosteric proteins; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 108; 9; 3-2011; 3499-35030027-8424CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1073/pnas.1018980108info:eu-repo/semantics/altIdentifier/url/https://www.pnas.org/content/108/9/3499info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:34:52Zoai:ri.conicet.gov.ar:11336/68870instacron: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 09:34:52.839CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
On the role of frustration in the energy landscapes of allosteric proteins |
title |
On the role of frustration in the energy landscapes of allosteric proteins |
spellingShingle |
On the role of frustration in the energy landscapes of allosteric proteins Ferreiro, Diego Minimal Frustration Principle Protein Folding Protein Function |
title_short |
On the role of frustration in the energy landscapes of allosteric proteins |
title_full |
On the role of frustration in the energy landscapes of allosteric proteins |
title_fullStr |
On the role of frustration in the energy landscapes of allosteric proteins |
title_full_unstemmed |
On the role of frustration in the energy landscapes of allosteric proteins |
title_sort |
On the role of frustration in the energy landscapes of allosteric proteins |
dc.creator.none.fl_str_mv |
Ferreiro, Diego Hegler, Joseph A. Komives, Elizabeth A. Wolynes, Peter G. |
author |
Ferreiro, Diego |
author_facet |
Ferreiro, Diego Hegler, Joseph A. Komives, Elizabeth A. Wolynes, Peter G. |
author_role |
author |
author2 |
Hegler, Joseph A. Komives, Elizabeth A. Wolynes, Peter G. |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
Minimal Frustration Principle Protein Folding Protein Function |
topic |
Minimal Frustration Principle Protein Folding Protein Function |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Natural protein domains must be sufficiently stable to fold but often need to be locally unstable to function. Overall, strong energetic conflicts are minimized in native states satisfying the principle of minimal frustration. Local violations of this principle open up possibilities to form the complex multifunnel energy landscapes needed for large-scale conformational changes. We survey the local frustration patterns of allosteric domains and show that the regions that reconfigure are often enriched in patches of highly frustrated interactions, consistent both with the idea that these locally frustrated regions may act as specific hinges or that proteins may "crack" in these locations. On the other hand, the symmetry of multimeric protein assemblies allows near degeneracy by reconfiguring while maintaining minimally frustrated interactions. We also anecdotally examine some specific examples of complex conformational changes and speculate on the role of frustration in the kinetics of allosteric change. 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; Argentina Fil: Hegler, Joseph A.. University of California at San Diego; Estados Unidos Fil: Komives, Elizabeth A.. University of California at San Diego; Estados Unidos Fil: Wolynes, Peter G.. University of California at San Diego; Estados Unidos |
description |
Natural protein domains must be sufficiently stable to fold but often need to be locally unstable to function. Overall, strong energetic conflicts are minimized in native states satisfying the principle of minimal frustration. Local violations of this principle open up possibilities to form the complex multifunnel energy landscapes needed for large-scale conformational changes. We survey the local frustration patterns of allosteric domains and show that the regions that reconfigure are often enriched in patches of highly frustrated interactions, consistent both with the idea that these locally frustrated regions may act as specific hinges or that proteins may "crack" in these locations. On the other hand, the symmetry of multimeric protein assemblies allows near degeneracy by reconfiguring while maintaining minimally frustrated interactions. We also anecdotally examine some specific examples of complex conformational changes and speculate on the role of frustration in the kinetics of allosteric change. |
publishDate |
2011 |
dc.date.none.fl_str_mv |
2011-03 |
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/11336/68870 Ferreiro, Diego; Hegler, Joseph A.; Komives, Elizabeth A.; Wolynes, Peter G.; On the role of frustration in the energy landscapes of allosteric proteins; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 108; 9; 3-2011; 3499-3503 0027-8424 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/68870 |
identifier_str_mv |
Ferreiro, Diego; Hegler, Joseph A.; Komives, Elizabeth A.; Wolynes, Peter G.; On the role of frustration in the energy landscapes of allosteric proteins; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 108; 9; 3-2011; 3499-3503 0027-8424 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1073/pnas.1018980108 info:eu-repo/semantics/altIdentifier/url/https://www.pnas.org/content/108/9/3499 |
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 |
National Academy of Sciences |
publisher.none.fl_str_mv |
National Academy of Sciences |
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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13.070432 |