Structural transitions in full-length human prion protein detected by xenon as probe and spin labeling of the N-terminal domain

URN to cite this document:: urn:nbn:de:bvb:355-epub-343998
DOI to cite this document:: 10.5283/epub.34399

Narayanan, Sunilkumar Puthenpurackal ; Nair, Divya Gopalakrishnan ; Schaal, Daniel ; de Aguiar, Marisa Barbosa ; Wenzel, Sabine ; Kremer, Werner ; Schwarzinger, Stephan ; Kalbitzer, Hans Robert

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Date of publication of this fulltext: 17 Aug 2016 14:41

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Abstract

Fatal neurodegenerative disorders termed transmissible spongiform encephalopathies (TSEs) are associated with the accumulation of fibrils of misfolded prion protein PrP. The noble gas xenon accommodates into four transiently enlarged hydrophobic cavities located in the well-folded core of human PrP(23-230) as detected by [H-1, N-15]-HSQC spectroscopy. In thermal equilibrium a fifth xenon binding ...