Data/hora: 06/06/2024 13:02:11

Provedor de dados: | 56
País: | Brazil
Título: | Volume and energy folding landscape of prion protein revealed by pressure
Autores: | Cordeiro,Y.; Kraineva,J.; Winter,R.; Silva,J.L.
Data: | 2005-08-01
Ano: | 2005
Palavras-chave: | Prion; High pressure; Structural conversion; Aggregation.
Resumo: | The main hypothesis for prion diseases proposes that the cellular protein (PrP C) can be altered into a misfolded, ß-sheet-rich isoform, the PrP Sc (from scrapie). The formation of this abnormal isoform then triggers the transmissible spongiform encephalopathies. Here, we discuss the use of high pressure as a tool to investigate this structural transition and to populate possible intermediates in the folding/unfolding pathway of the prion protein. The latest findings on the application of high pressure to the cellular prion protein and to the scrapie PrP forms will be summarized in this review, which focuses on the energetic and volumetric properties of prion folding and conversion.
Tipo: | Info:eu-repo/semantics/article
Idioma: | Inglês
Identificador: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000800006
Editor: | Associação Brasileira de Divulgação Científica
Relação: | 10.1590/S0100-879X2005000800006
Formato: | text/html
Fonte: | Brazilian Journal of Medical and Biological Research  v.38 n.8 2005
Fonte: | info:eu-repo/semantics/openAccess