On the role of frustration in the energy landscapes of allosteric proteins

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 comp...

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Detalles Bibliográficos
Autores: Ferreiro, Diego, Hegler, Joseph A., Komives, Elizabeth A., Wolynes, Peter G.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2011
País:Argentina
Institución:Consejo Nacional de Investigaciones Científicas y Técnicas
Repositorio:CONICET Digital (CONICET)
Idioma:inglés
OAI Identifier:oai:ri.conicet.gov.ar:11336/68870
Acceso en línea:http://hdl.handle.net/11336/68870
Access Level:acceso abierto
Palabra clave:Minimal Frustration Principle
Protein Folding
Protein Function
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
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spelling 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 Técnicas2024-05-08T13:34:04Zoai: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:34982024-05-08 13:34:04.82CONICET 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
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
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
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
topic Minimal Frustration Principle
Protein Folding
Protein Function
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
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
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
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score 15,812429

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