Probing the Energy Landscape of Spectrin R15 and R16 and the Effects of Non-native Interactions

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Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.contributorUniversity of Maryland School of Pharmacy-
Autor(es): dc.contributorRice University-
Autor(es): dc.creatorda Silva, Fernando Bruno-
Autor(es): dc.creatorMartins de Oliveira, Vinícius-
Autor(es): dc.creatorde Oliveira Junior, Antonio Bento-
Autor(es): dc.creatorContessoto, Vinícius de Godoi-
Autor(es): dc.creatorLeite, Vitor B. P.-
Data de aceite: dc.date.accessioned2025-08-21T22:46:46Z-
Data de disponibilização: dc.date.available2025-08-21T22:46:46Z-
Data de envio: dc.date.issued2023-07-29-
Data de envio: dc.date.issued2023-07-29-
Data de envio: dc.date.issued2023-02-15-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1021/acs.jpcb.2c06178-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/246774-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/246774-
Descrição: dc.descriptionUnderstanding the details of a protein folding mechanism can be a challenging and complex task. One system with an interesting folding behavior is the α-spectrin domain, where the R15 folds three-orders of magnitude faster than its homologues R16 and R17, despite having similar structures. The molecular origins that explain these folding rate differences remain unclear, but our previous work revealed that a combined effect produced by non-native interactions could be a reasonable cause for these differences. In this study, we explore further the folding process by identifying the molecular paths, metastable states, and the collective motions that lead these unfolded proteins to their native state conformation. Our results uncovered the differences between the folding pathways for the wild-type R15 and R16 and an R16 mutant. The metastable ensembles that speed down the folding were identified using an energy landscape visualization method (ELViM). These ensembles correspond to similar experimentally reported configurations. Our observations indicate that the non-native interactions are also associated with secondary structure misdocking. This computational methodology can be used as a fast, straightforward protocol for shedding light on systems with unclear folding or conformational traps.-
Descrição: dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)-
Descrição: dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
Descrição: dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
Descrição: dc.descriptionDepartment of Physics São Paulo State University (UNESP) Institute of Biosciences Humanities and Exact Sciences, São Paulo-
Descrição: dc.descriptionDepartment of Pharmaceutical Sciences University of Maryland School of Pharmacy-
Descrição: dc.descriptionCenter for Theoretical Biological Physics Rice University-
Descrição: dc.descriptionDepartment of Physics São Paulo State University (UNESP) Institute of Biosciences Humanities and Exact Sciences, São Paulo-
Formato: dc.format1291-1300-
Idioma: dc.languageen-
Relação: dc.relationJournal of Physical Chemistry B-
???dc.source???: dc.sourceScopus-
Título: dc.titleProbing the Energy Landscape of Spectrin R15 and R16 and the Effects of Non-native Interactions-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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