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
- Institución
- Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
- OAI Identificador
- paperaa:paper_00278424_v108_n9_p3499_Ferreiro
Ver los metadatos del registro completo
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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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1846142849833238528 |
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12.712165 |