Analyzing the effect of homogeneous frustration in protein folding

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dc.contributor.authorContessoto, Vinícius G. [UNESP]
dc.contributor.authorLima, Debora T. [UNESP]
dc.contributor.authorOliveira, Ronaldo J. [UNESP]
dc.contributor.authorBruni, Aline T.
dc.contributor.authorChahine, Jorge [UNESP]
dc.contributor.authorLeite, Vitor Barbanti Pereira [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionLaboratório Nacional de Ciência e Tecnologia do Bioetanol, Campinas
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.date.accessioned2014-05-27T11:30:46Z
dc.date.available2014-05-27T11:30:46Z
dc.date.issued2013-10-01
dc.description.abstractThe energy landscape theory has been an invaluable theoretical framework in the understanding of biological processes such as protein folding, oligomerization, and functional transitions. According to the theory, the energy landscape of protein folding is funneled toward the native state, a conformational state that is consistent with the principle of minimal frustration. It has been accepted that real proteins are selected through natural evolution, satisfying the minimum frustration criterion. However, there is evidence that a low degree of frustration accelerates folding. We examined the interplay between topological and energetic protein frustration. We employed a Cα structure-based model for simulations with a controlled nonspecific energetic frustration added to the potential energy function. Thermodynamics and kinetics of a group of 19 proteins are completely characterized as a function of increasing level of energetic frustration. We observed two well-separated groups of proteins: one group where a little frustration enhances folding rates to an optimal value and another where any energetic frustration slows down folding. Protein energetic frustration regimes and their mechanisms are explained by the role of non-native contact interactions in different folding scenarios. These findings strongly correlate with the protein free-energy folding barrier and the absolute contact order parameters. These computational results are corroborated by principal component analysis and partial least square techniques. One simple theoretical model is proposed as a useful tool for experimentalists to predict the limits of improvements in real proteins. © 2013 Wiley Periodicals, Inc.en
dc.description.affiliationDepartamento de Física Instituto de Biociências, Letras e Ciências Exatas Universidade Estadual Paulista, Sao José do Rio Preto, São Paulo, 15054-000
dc.description.affiliationLaboratório Nacional de Ciência e Tecnologia do Bioetanol, Campinas, São Paulo, 13083-970
dc.description.affiliationDepartamento de Química Faculdade de Filosofia Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, São Paulo
dc.description.affiliationUnespDepartamento de Física Instituto de Biociências, Letras e Ciências Exatas Universidade Estadual Paulista, Sao José do Rio Preto, São Paulo, 15054-000
dc.format.extent1727-1737
dc.identifierhttp://dx.doi.org/10.1002/prot.24309
dc.identifier.citationProteins: Structure, Function and Bioinformatics, v. 81, n. 10, p. 1727-1737, 2013.
dc.identifier.doi10.1002/prot.24309
dc.identifier.issn0887-3585
dc.identifier.issn1097-0134
dc.identifier.lattes1518826294347383
dc.identifier.lattes0500034174785796
dc.identifier.scopus2-s2.0-84884205766
dc.identifier.urihttp://hdl.handle.net/11449/76681
dc.identifier.wosWOS:000324115400005
dc.language.isoeng
dc.relation.ispartofProteins: Structure, Function and Bioinformatics
dc.relation.ispartofjcr2.274
dc.relation.ispartofsjr1,362
dc.relation.ispartofsjr1,362
dc.rights.accessRightsAcesso restrito
dc.sourceScopus
dc.subjectC-alpha model
dc.subjectMolecular dynamics
dc.subjectMultivariate analysis
dc.subjectStructure-based model
dc.subjectpriority journal
dc.subjectprotein conformation
dc.subjectprotein folding
dc.subjectprotein frustration
dc.subjectprotein interaction
dc.subjectprotein localization
dc.subjectprotein motif
dc.subjectthermodynamics
dc.subjectthermostability
dc.subjecttransition temperature
dc.titleAnalyzing the effect of homogeneous frustration in protein foldingen
dc.typeArtigo
dcterms.licensehttp://olabout.wiley.com/WileyCDA/Section/id-406071.html
unesp.author.lattes1518826294347383
unesp.author.lattes0500034174785796
unesp.author.orcid0000-0003-4860-309X[3]
unesp.author.orcid0000-0002-1891-9563[1]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt

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