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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Detalles Bibliográficos
Autores principales: Ferreiro, D.U., Hegler, J.A., Komives, E.A., Wolynes, P.G.
Formato: Artículo publishedVersion
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
http://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00278424_v108_n9_p3499_Ferreiro_oai
Aporte de:
Repositorio Digital de la Universidad de Buenos Aires (UBA) de Universidad de Buenos Aires

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