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

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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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Autores principales:	Ferreiro, D.U., Hegler, J.A., Komives, E.A., Wolynes, P.G.
Formato:	Artículo publishedVersion
Lenguaje:	Inglés
Publicado:	2011
Materias:	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
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_00278424_v108_n9_p3499_Ferreiro
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paperaa:paper_00278424_v108_n9_p3499_Ferreiro
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spelling	paperaa:paper_00278424_v108_n9_p3499_Ferreiro2023-06-12T16:45:19Z On the role of frustration in the energy landscapes of allosteric proteins Proc. Natl. Acad. Sci. U. S. A. 2011;108(9):3499-3503 Ferreiro, D.U. Hegler, J.A. Komives, E.A. Wolynes, P.G. 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 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. 2011 info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion application/pdf eng info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00278424_v108_n9_p3499_Ferreiro
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
language	Inglés
orig_language_str_mv	eng
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
spellingShingle	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 Ferreiro, D.U. Hegler, J.A. Komives, E.A. Wolynes, P.G. On the role of frustration in the energy landscapes of allosteric proteins
topic_facet	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
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.
format	Artículo Artículo publishedVersion
author	Ferreiro, D.U. Hegler, J.A. Komives, E.A. Wolynes, P.G.
author_facet	Ferreiro, D.U. Hegler, J.A. Komives, E.A. Wolynes, P.G.
author_sort	Ferreiro, D.U.
title	On the role of frustration in the energy landscapes of allosteric proteins
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
publishDate	2011
url	http://hdl.handle.net/20.500.12110/paper_00278424_v108_n9_p3499_Ferreiro
work_keys_str_mv	AT ferreirodu ontheroleoffrustrationintheenergylandscapesofallostericproteins AT heglerja ontheroleoffrustrationintheenergylandscapesofallostericproteins AT komivesea ontheroleoffrustrationintheenergylandscapesofallostericproteins AT wolynespg ontheroleoffrustrationintheenergylandscapesofallostericproteins
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On the role of frustration in the energy landscapes of allosteric proteins

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