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.
Registro:
Documento: |
Artículo
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Título: | On the role of frustration in the energy landscapes of allosteric proteins |
Autor: | Ferreiro, D.U.; Hegler, J.A.; Komives, E.A.; Wolynes, P.G. |
Filiación: | Department of Biological Chemistry, Facultad de Ciencias Exactas Y Naturales, Universidad de Buenos Aires, Buenos Aires, C1428EGA, Argentina Department of Chemistry and Biochemistry, University of California at San Diego, San Diego, CA 92107, United States Center for Theoretical Biological Physics, University of California at San Diego, San Diego, CA 92107, United States
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Palabras clave: | 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 |
Año: | 2011
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Volumen: | 108
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Número: | 9
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Página de inicio: | 3499
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Página de fin: | 3503
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DOI: |
http://dx.doi.org/10.1073/pnas.1018980108 |
Título revista: | Proceedings of the National Academy of Sciences of the United States of America
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Título revista abreviado: | Proc. Natl. Acad. Sci. U. S. A.
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ISSN: | 00278424
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CODEN: | PNASA
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CAS: | Amino Acids; Proteins
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PDF: | https://bibliotecadigital.exactas.uba.ar/download/paper/paper_00278424_v108_n9_p3499_Ferreiro.pdf |
Registro: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00278424_v108_n9_p3499_Ferreiro |
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Citas:
---------- APA ----------
Ferreiro, D.U., Hegler, J.A., Komives, E.A. & Wolynes, P.G.
(2011)
. On the role of frustration in the energy landscapes of allosteric proteins. Proceedings of the National Academy of Sciences of the United States of America, 108(9), 3499-3503.
http://dx.doi.org/10.1073/pnas.1018980108---------- CHICAGO ----------
Ferreiro, D.U., Hegler, J.A., Komives, E.A., Wolynes, P.G.
"On the role of frustration in the energy landscapes of allosteric proteins"
. Proceedings of the National Academy of Sciences of the United States of America 108, no. 9
(2011) : 3499-3503.
http://dx.doi.org/10.1073/pnas.1018980108---------- MLA ----------
Ferreiro, D.U., Hegler, J.A., Komives, E.A., Wolynes, P.G.
"On the role of frustration in the energy landscapes of allosteric proteins"
. Proceedings of the National Academy of Sciences of the United States of America, vol. 108, no. 9, 2011, pp. 3499-3503.
http://dx.doi.org/10.1073/pnas.1018980108---------- VANCOUVER ----------
Ferreiro, D.U., Hegler, J.A., Komives, E.A., Wolynes, P.G. On the role of frustration in the energy landscapes of allosteric proteins. Proc. Natl. Acad. Sci. U. S. A. 2011;108(9):3499-3503.
http://dx.doi.org/10.1073/pnas.1018980108