Observation of intermediate states of the human prion protein by high pressure NMR spectroscopy

DOI to cite this document:: 10.5283/epub.1886

Kachel, Norman ; Kremer, Werner ; Zahn, Ralph ; Kalbitzer, Hans-Robert

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Date of publication of this fulltext: 05 Aug 2009 13:34

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Abstract

Background Prions as causative agents of transmissible spongiform encephalopathies (TSEs) in humans and animals are composed of the infectious isomer, PrPSc, of the cellular prion protein, PrPC. The conversion and thus the propensity of PrPC to adopt alternative folds leads to the species-specific propagation of the disease. High pressure is a powerful tool to study the physico-chemical ...