Volume and energy folding landscape of prion protein revealed by pressure
Braz. j. med. biol. res
; 38(8): 1195-1201, Aug. 2005. ilus, tab
Artículo
en Inglés
| LILACS
| ID: lil-405520
Biblioteca responsable:
BR1.1
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.
Texto completo:
Disponible
Colección:
Bases de datos internacionales
Base de datos:
LILACS
Asunto principal:
Presión
/
Priones
/
Pliegue de Proteína
Límite:
Animales
/
Humanos
Idioma:
Inglés
Revista:
Braz. j. med. biol. res
Asunto de la revista:
Biologia
/
Medicina
Año:
2005
Tipo del documento:
Artículo
/
Congreso y conferencia
País de afiliación:
Brasil
/
Alemania
Institución/País de afiliación:
Universidade Federal do Rio de Janeiro/BR
/
University of Dortmund/DE