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• W2092192893 abstract "Hard core: We have analyzed the structural rearrangements of the urea-denatured state of recombinant prion protein by using liquid-state NMR spectroscopy. Our studies document that prion amyloid fibrils generated from monomeric, urea-unfolded human prion protein have a rigid core between residues 145–223. Detailed facts of importance to specialist readers are published as ”Supporting Information”. Such documents are peer-reviewed, but not copy-edited or typeset. They are made available as submitted by the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article." @default.
• W2092192893 created "2016-06-24" @default.
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• W2092192893 date "2010-06-07" @default.
• W2092192893 modified "2023-10-18" @default.
• W2092192893 title "Prion Protein Amyloid Formation Involves Structural Rearrangements in the C-Terminal Domain" @default.
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• W2092192893 doi "https://doi.org/10.1002/cbic.201000076" @default.
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• W2092192893 hasPublicationYear "2010" @default.
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