Volume and energy folding landscape of prion protein revealed by pressure

Brazilian Journal of Medical and Biological Research. 2005;38(8):1195-1201 DOI 10.1590/S0100-879X2005000800006

 

Journal Homepage

Journal Title: Brazilian Journal of Medical and Biological Research

ISSN: 0100-879X (Print); 1414-431X (Online)

Publisher: Associação Brasileira de Divulgação Científica

Society/Institution: Associação Brasileira de Divulgação Científica

LCC Subject Category: Medicine: Medicine (General) | Science: Biology (General)

Country of publisher: Brazil

Language of fulltext: English

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AUTHORS

Y. Cordeiro
J. Kraineva
R. Winter
J.L. Silva

EDITORIAL INFORMATION

Peer review

Editorial Board

Instructions for authors

Time From Submission to Publication: 22 weeks

 

Abstract | Full Text

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.