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dc.contributor.author
Ferreiro, Diego
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dc.contributor.author
Hegler, Joseph A.
dc.contributor.author
Komives, Elizabeth A.
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dc.contributor.author
Wolynes, Peter G.
dc.date.available
2019-01-29T18:02:56Z
dc.date.issued
2011-03
dc.identifier.citation
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
dc.identifier.issn
0027-8424
dc.identifier.uri
http://hdl.handle.net/11336/68870
dc.description.abstract
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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
National Academy of Sciences
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Minimal Frustration Principle
dc.subject
Protein Folding
dc.subject
Protein Function
dc.subject.classification
Otras Ciencias Biológicas
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
On the role of frustration in the energy landscapes of allosteric proteins
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-01-14T18:32:17Z
dc.journal.volume
108
dc.journal.number
9
dc.journal.pagination
3499-3503
dc.journal.pais
Estados Unidos
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dc.description.fil
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
dc.description.fil
Fil: Hegler, Joseph A.. University of California at San Diego; Estados Unidos
dc.description.fil
Fil: Komives, Elizabeth A.. University of California at San Diego; Estados Unidos
dc.description.fil
Fil: Wolynes, Peter G.. University of California at San Diego; Estados Unidos
dc.journal.title
Proceedings of the National Academy of Sciences of The United States of America
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1073/pnas.1018980108
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.pnas.org/content/108/9/3499
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