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A Hooke's law-based approach to protein folding rate

dc.creatorRuiz-Blanco Y.B.
dc.creatorMarrero-Ponce Y.
dc.creatorPrieto P.J.
dc.creatorSalgado J.
dc.creatorGarcía Y.
dc.creatorSotomayor-Torres C.M.
dc.date.accessioned2020-03-26T16:32:47Z
dc.date.available2020-03-26T16:32:47Z
dc.date.issued2015
dc.identifier.citationJournal of Theoretical Biology; Vol. 364, pp. 407-417
dc.identifier.issn00225193
dc.identifier.urihttps://hdl.handle.net/20.500.12585/9020
dc.description.abstractKinetics is a key aspect of the renowned protein folding problem. Here, we propose a comprehensive approach to folding kinetics where a polypeptide chain is assumed to behave as an elastic material described by the Hooke[U+05F3]s law. A novel parameter called elastic-folding constant results from our model and is suggested to distinguish between protein with two-state and multi-state folding pathways. A contact-free descriptor, named folding degree, is introduced as a suitable structural feature to study protein-folding kinetics. This approach generalizes the observed correlations between varieties of structural descriptors with the folding rate constant. Additionally several comparisons among structural classes and folding mechanisms were carried out showing the good performance of our model with proteins of different types. The present model constitutes a simple rationale for the structural and energetic factors involved in protein folding kinetics. © 2014 Elsevier Ltd.eng
dc.format.mediumRecurso electrónico
dc.format.mimetypeapplication/pdf
dc.language.isoeng
dc.publisherAcademic Press
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.sourcehttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84910086539&doi=10.1016%2fj.jtbi.2014.09.002&partnerID=40&md5=d32479becf63730a4252ec30e659e982
dc.titleA Hooke's law-based approach to protein folding rate
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datacite.rightshttp://purl.org/coar/access_right/c_16ec
oaire.resourceTypehttp://purl.org/coar/resource_type/c_6501
oaire.versionhttp://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.driverinfo:eu-repo/semantics/article
dc.type.hasversioninfo:eu-repo/semantics/publishedVersion
dc.identifier.doi10.1016/j.jtbi.2014.09.002
dc.subject.keywordsElastic folding constant
dc.subject.keywordsFolding degree
dc.subject.keywordsFolding kinetics
dc.subject.keywordsPROTDCAL
dc.subject.keywordsPolypeptide
dc.subject.keywordsDNA
dc.subject.keywordsProtein
dc.subject.keywordsEnergetics
dc.subject.keywordsModeling
dc.subject.keywordsPeptide
dc.subject.keywordsProtein
dc.subject.keywordsReaction kinetics
dc.subject.keywordsAmino acid sequence
dc.subject.keywordsArticle
dc.subject.keywordsElasticity
dc.subject.keywordsProtein folding
dc.subject.keywordsProtein structure
dc.subject.keywordsStructure analysis
dc.subject.keywordsTheoretical model
dc.subject.keywordsChemical model
dc.subject.keywordsChemistry
dc.subject.keywordsComputer simulation
dc.subject.keywordsKinetics
dc.subject.keywordsProtein secondary structure
dc.subject.keywordsThermodynamics
dc.subject.keywordsComputer simulation
dc.subject.keywordsDNA
dc.subject.keywordsKinetics
dc.subject.keywordsModels, Chemical
dc.subject.keywordsProtein folding
dc.subject.keywordsProtein Structure, Secondary
dc.subject.keywordsProteins
dc.subject.keywordsThermodynamics
dc.rights.accessrightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.ccAtribución-NoComercial 4.0 Internacional
dc.identifier.instnameUniversidad Tecnológica de Bolívar
dc.identifier.reponameRepositorio UTB
dc.description.notesDNA, 9007-49-2; protein, 67254-75-5; DNA; Proteins
dc.type.spaArtículo
dc.identifier.orcid36933887400
dc.identifier.orcid55665599200
dc.identifier.orcid53878266200
dc.identifier.orcid7102811634
dc.identifier.orcid36945042600
dc.identifier.orcid35403074800


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