Small Neutral Crowding Solute Effects on Protein Folding Thermodynamic Stability and Kinetics

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Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.contributorUniversidade Federal do Triângulo Mineiro-
Autor(es): dc.creatorContessoto, Vinícius G.-
Autor(es): dc.creatorFerreira, Paulo H. B.-
Autor(es): dc.creatorChahine, Jorge-
Autor(es): dc.creatorLeite, Vitor B. P.-
Autor(es): dc.creatorOliveira, Ronaldo J.-
Data de aceite: dc.date.accessioned2025-08-21T19:00:20Z-
Data de disponibilização: dc.date.available2025-08-21T19:00:20Z-
Data de envio: dc.date.issued2022-05-01-
Data de envio: dc.date.issued2022-05-01-
Data de envio: dc.date.issued2021-10-27-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1021/acs.jpcb.1c07663-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/233756-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/233756-
Descrição: dc.descriptionMolecular crowding is a ubiquitous phenomenon in biological systems, with significant consequences on protein folding and stability. Small compounds, such as the osmolyte trimethylamineN-oxide (TMAO), can also present similar effects. To analyze the effects arising from these solute-like molecules, we performed a series of crowded coarse-grained folding simulations. Two well-known proteins were chosen, CI2 and SH3, modeled by the alpha-carbon-structure-based model. In the simulations, the crowding molecules were represented by low-sized neutral atom beads in different concentrations. The results show that a low level of the volume fraction occupied by neutral agents can change protein stability and folding kinetics for the two systems. However, the kinetics were shown to be unaffected in their respective folding temperatures. The faster kinetics correlates with changes in the folding route for systems at the same temperature, where non-native contacts were shown to be relevant. The transition states of the two systems with and without crowders are similar. In the case of SH3, there are differences in the structuring of two strands, which may be associated with the increase in its folding rate, in addition to the destabilization of the denatured ensemble. The present study also detected a crossover in the thermodynamic stability behavior, previously observed experimentally and theoretically. As the temperature increases, crowders change from destabilizing to stabilizing agents.-
Descrição: dc.descriptionDepartment of Physics Institute of Biosciences Letters and Exact Sciences São Paulo State University-
Descrição: dc.descriptionLaboratório de Biofísica Teórica Departamento de Física Instituto de Ciências Exatas Naturais e Educação Universidade Federal do Triângulo Mineiro-
Descrição: dc.descriptionDepartment of Physics Institute of Biosciences Letters and Exact Sciences São Paulo State University-
Formato: dc.format11673-11686-
Idioma: dc.languageen-
Relação: dc.relationJournal of Physical Chemistry B-
???dc.source???: dc.sourceScopus-
Título: dc.titleSmall Neutral Crowding Solute Effects on Protein Folding Thermodynamic Stability and Kinetics-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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