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dc.contributor.authorDe Oliveira, Vinícius M.
dc.contributor.authorCaetano, Daniel L. Z. [UNESP]
dc.contributor.authorDa Silva, Fernando B. [UNESP]
dc.contributor.authorMouro, Paulo R. [UNESP]
dc.contributor.authorDe Oliveira, Antonio B. [UNESP]
dc.contributor.authorDe Carvalho, Sidney J. [UNESP]
dc.contributor.authorLeite, Vitor B. P. [UNESP]
dc.date.accessioned2020-12-12T01:11:37Z
dc.date.available2020-12-12T01:11:37Z
dc.date.issued2020-01-14
dc.identifierhttp://dx.doi.org/10.1021/acs.jctc.9b00894
dc.identifier.citationJournal of Chemical Theory and Computation, v. 16, n. 1, p. 765-772, 2020.
dc.identifier.issn1549-9626
dc.identifier.issn1549-9618
dc.identifier.urihttp://hdl.handle.net/11449/198393
dc.description.abstractThe folding and stability of proteins is a fundamental problem in several research fields. In the present paper, we have used different computational approaches to study the effects caused by changes in pH and for charged mutations in cold shock proteins from Bacillus subtilis (Bs-CspB). First, we have investigated the contribution of each ionizable residue for these proteins to their thermal stability using the TKSA-MC, a Web server for rational mutation via optimizing the protein charge interactions. Based on these results, we have proposed a new mutation in an already optimized Bs-CspB variant. We have evaluated the effects of this new mutation in the folding energy landscape using structure-based models in Monte Carlo simulation at constant pH, SBM-CpHMC. Our results using this approach have indicated that the charge rearrangements already in the unfolded state are critical to the thermal stability of Bs-CspB. Furthermore, the conjunction of these simplified methods was able not only to predict stabilizing mutations in different pHs but also to provide essential information about their effects in each stage of protein folding.en
dc.format.extent765-772
dc.language.isoeng
dc.relation.ispartofJournal of Chemical Theory and Computation
dc.sourceScopus
dc.titlePH and Charged Mutations Modulate Cold Shock Protein Folding and Stability: A Constant pH Monte Carlo Studyen
dc.typeArtigo
dc.contributor.institutionLNBio/CNPEM
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionRice University
dc.description.affiliationBrazilian Biosciences National Laboratory National Center for Research in Energy and Materials LNBio/CNPEM
dc.description.affiliationDepartment of Physics Saõ Paulo State University (UNESP) Institute of Biosciences Humanities and Exact Sciences
dc.description.affiliationCenter for Theoretical Biological Physics Rice University
dc.description.affiliationUnespDepartment of Physics Saõ Paulo State University (UNESP) Institute of Biosciences Humanities and Exact Sciences
dc.identifier.doi10.1021/acs.jctc.9b00894
dc.identifier.scopus2-s2.0-85077790042
unesp.author.orcid0000-0003-0927-3825[1]
unesp.author.orcid0000-0002-0476-3115[2]
unesp.author.orcid0000-0002-0285-8700[3]
unesp.author.orcid0000-0003-0008-9079 0000-0003-0008-9079[7]
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