TKSA-MC: A web server for rational mutation through the optimization of protein charge interactions

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dc.contributor.authorContessoto, Vinícius G. [UNESP]
dc.contributor.authorde Oliveira, Vinícius M. [UNESP]
dc.contributor.authorFernandes, Bruno R. [UNESP]
dc.contributor.authorSlade, Gabriel G. [UNESP]
dc.contributor.authorLeite, Vitor B. P. [UNESP]
dc.contributor.institutionBrazilian Bioethanol Science and Technology Laboratory – CTBE
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade Federal do Triângulo Mineiro – UFTM
dc.date.accessioned2019-10-06T15:19:06Z
dc.date.available2019-10-06T15:19:06Z
dc.date.issued2018-11-01
dc.description.abstractThe TKSAMC is a web server which calculates protein charge–charge interactions via the Tanford–Kirkwood Surface Accessibility model with the Monte Carlo method for sampling different protein protonation states. The optimization of charge–charge interactions via directed mutations has successfully enhanced the thermal stability of different proteins and could be a key to protein engineering improvement. The server presents the electrostatic free energy contribution of each polar-charged residue to the protein native state stability. Specific residues are suggested to be mutated for improving thermal stability. The choice of a residue is based on its fraction of side chain exposed to solvent and its positive free energy contribution, which tends to destabilize the protein native state. Any residue energy contribution can be shown as a function of pH condition. The web server is freely available at UNESP (São Paulo State University - DF/IBILCE): http://tksamc.df.ibilce.unesp.br and also on GitHub https://github.com/contessoto/tksamc.en
dc.description.affiliationBrazilian Bioethanol Science and Technology Laboratory – CTBE
dc.description.affiliationDepartment of Physics Institute of Biosciences Letters and Exact Sciences São Paulo State University – UNESP
dc.description.affiliationTheoretical Biophysics Laboratory Departamento de Física Instituto de Ciências Exatas Naturais e Educação Universidade Federal do Triângulo Mineiro – UFTM
dc.description.affiliationUnespDepartment of Physics Institute of Biosciences Letters and Exact Sciences São Paulo State University – UNESP
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipIdCNPq: 167374/2017-6
dc.description.sponsorshipIdFAPESP: 2014/06862-7
dc.description.sponsorshipIdFAPESP: 2016/13998-8
dc.description.sponsorshipIdFAPESP: 2016/19766-1
dc.description.sponsorshipIdFAPESP: 2017/09662-7
dc.format.extent1184-1188
dc.identifierhttp://dx.doi.org/10.1002/prot.25599
dc.identifier.citationProteins: Structure, Function and Bioinformatics, v. 86, n. 11, p. 1184-1188, 2018.
dc.identifier.doi10.1002/prot.25599
dc.identifier.issn1097-0134
dc.identifier.issn0887-3585
dc.identifier.scopus2-s2.0-85053871598
dc.identifier.urihttp://hdl.handle.net/11449/186894
dc.language.isoeng
dc.relation.ispartofProteins: Structure, Function and Bioinformatics
dc.rights.accessRightsAcesso restrito
dc.sourceScopus
dc.subjectcharge–charge interaction
dc.subjectprotein engineering
dc.subjectprotein thermal stability
dc.subjectrational mutation
dc.subjectTSKA model
dc.subjectweb server
dc.titleTKSA-MC: A web server for rational mutation through the optimization of protein charge interactionsen
dc.typeArtigo
unesp.author.orcid0000-0002-1891-9563[1]
unesp.author.orcid0000-0003-0927-3825[2]

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