PH and Charged Mutations Modulate Cold Shock Protein Folding and Stability: A Constant pH Monte Carlo Study

Registro completo de metadados
MetadadosDescriçãoIdioma
Autor(es): dc.contributorLNBio/CNPEM-
Autor(es): dc.contributorUniversidade Estadual Paulista (Unesp)-
Autor(es): dc.contributorRice University-
Autor(es): dc.creatorDe Oliveira, Vinícius M.-
Autor(es): dc.creatorCaetano, Daniel L. Z. [UNESP]-
Autor(es): dc.creatorDa Silva, Fernando B. [UNESP]-
Autor(es): dc.creatorMouro, Paulo R. [UNESP]-
Autor(es): dc.creatorDe Oliveira, Antonio B. [UNESP]-
Autor(es): dc.creatorDe Carvalho, Sidney J. [UNESP]-
Autor(es): dc.creatorLeite, Vitor B. P. [UNESP]-
Data de aceite: dc.date.accessioned2022-02-22T00:24:24Z-
Data de disponibilização: dc.date.available2022-02-22T00:24:24Z-
Data de envio: dc.date.issued2020-12-11-
Data de envio: dc.date.issued2020-12-11-
Data de envio: dc.date.issued2020-01-13-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1021/acs.jctc.9b00894-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/198393-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/198393-
Descrição: dc.descriptionThe 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.-
Descrição: dc.descriptionBrazilian Biosciences National Laboratory National Center for Research in Energy and Materials LNBio/CNPEM-
Descrição: dc.descriptionDepartment of Physics Saõ Paulo State University (UNESP) Institute of Biosciences Humanities and Exact Sciences-
Descrição: dc.descriptionCenter for Theoretical Biological Physics Rice University-
Descrição: dc.descriptionDepartment of Physics Saõ Paulo State University (UNESP) Institute of Biosciences Humanities and Exact Sciences-
Formato: dc.format765-772-
Idioma: dc.languageen-
Relação: dc.relationJournal of Chemical Theory and Computation-
???dc.source???: dc.sourceScopus-
Título: dc.titlePH and Charged Mutations Modulate Cold Shock Protein Folding and Stability: A Constant pH Monte Carlo Study-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

Não existem arquivos associados a este item.