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

Autores
Ferreiro, D.U.; Hegler, J.A.; Komives, E.A.; Wolynes, P.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, D.U. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fuente
Proc. Natl. Acad. Sci. U. S. A. 2011;108(9):3499-3503
Materia
Minimal frustration principle
Protein folding
Protein function
article
priority journal
protein analysis
protein assembly
protein domain
protein interaction
protein localization
protein structure
Allosteric Regulation
Amino Acids
Databases, Protein
Models, Molecular
Protein Structure, Secondary
Protein Structure, Tertiary
Proteins
Thermodynamics
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/2.5/ar
Repositorio
Biblioteca Digital (UBA-FCEN)
Institución
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
OAI Identificador
paperaa:paper_00278424_v108_n9_p3499_Ferreiro

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oai_identifier_str paperaa:paper_00278424_v108_n9_p3499_Ferreiro
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling On the role of frustration in the energy landscapes of allosteric proteinsFerreiro, D.U.Hegler, J.A.Komives, E.A.Wolynes, P.G.Minimal frustration principleProtein foldingProtein functionarticlepriority journalprotein analysisprotein assemblyprotein domainprotein interactionprotein localizationprotein structureAllosteric RegulationAmino AcidsDatabases, ProteinModels, MolecularProtein Structure, SecondaryProtein Structure, TertiaryProteinsThermodynamicsNatural 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, D.U. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.2011info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12110/paper_00278424_v108_n9_p3499_FerreiroProc. Natl. Acad. Sci. U. S. A. 2011;108(9):3499-3503reponame:Biblioteca Digital (UBA-FCEN)instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesinstacron:UBA-FCENenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/ar2025-10-16T09:30:20Zpaperaa:paper_00278424_v108_n9_p3499_FerreiroInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-10-16 09:30:22.137Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
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, D.U.
Minimal frustration principle
Protein folding
Protein function
article
priority journal
protein analysis
protein assembly
protein domain
protein interaction
protein localization
protein structure
Allosteric Regulation
Amino Acids
Databases, Protein
Models, Molecular
Protein Structure, Secondary
Protein Structure, Tertiary
Proteins
Thermodynamics
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, D.U.
Hegler, J.A.
Komives, E.A.
Wolynes, P.G.
author Ferreiro, D.U.
author_facet Ferreiro, D.U.
Hegler, J.A.
Komives, E.A.
Wolynes, P.G.
author_role author
author2 Hegler, J.A.
Komives, E.A.
Wolynes, P.G.
author2_role author
author
author
dc.subject.none.fl_str_mv Minimal frustration principle
Protein folding
Protein function
article
priority journal
protein analysis
protein assembly
protein domain
protein interaction
protein localization
protein structure
Allosteric Regulation
Amino Acids
Databases, Protein
Models, Molecular
Protein Structure, Secondary
Protein Structure, Tertiary
Proteins
Thermodynamics
topic Minimal frustration principle
Protein folding
Protein function
article
priority journal
protein analysis
protein assembly
protein domain
protein interaction
protein localization
protein structure
Allosteric Regulation
Amino Acids
Databases, Protein
Models, Molecular
Protein Structure, Secondary
Protein Structure, Tertiary
Proteins
Thermodynamics
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, D.U. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
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
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/20.500.12110/paper_00278424_v108_n9_p3499_Ferreiro
url http://hdl.handle.net/20.500.12110/paper_00278424_v108_n9_p3499_Ferreiro
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/2.5/ar
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/2.5/ar
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv Proc. Natl. Acad. Sci. U. S. A. 2011;108(9):3499-3503
reponame:Biblioteca Digital (UBA-FCEN)
instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron:UBA-FCEN
reponame_str Biblioteca Digital (UBA-FCEN)
collection Biblioteca Digital (UBA-FCEN)
instname_str Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron_str UBA-FCEN
institution UBA-FCEN
repository.name.fl_str_mv Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
repository.mail.fl_str_mv ana@bl.fcen.uba.ar
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