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

Narayanan, Sunilkumar Puthenpurackal, Nair, Divya Gopalakrishnan, Schaal, Daniel, de Aguiar, Marisa Barbosa, Wenzel, Sabine, Kremer, Werner, Schwarzinger, Stephan and Kalbitzer, Hans Robert (2016) Structural transitions in full-length human prion protein detected by xenon as probe and spin labeling of the N-terminal domain. Scientific Reports 6 (28419), pp. 1-17.

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

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Other URL: http://www.nature.com/articles/srep28419


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 [1H, 15N]-HSQC spectroscopy. In thermal equilibrium a fifth xenon binding ...

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Item type:Article
Date:24 June 2016
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Projects:Open Access Publizieren (DFG)
Identification Number:
ValueType
10.1038/srep28419DOI
Dewey Decimal Classification:500 Science > 570 Life sciences
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Item ID:34399
Owner only: item control page

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