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• W3196857826 startingPage "9635" @default.
• W3196857826 abstract "Prion diseases are associated with conformational conversion of cellular prion protein into a misfolded pathogenic form, which resembles many properties of amyloid fibrils. The same prion protein sequence can misfold into different conformations, which are responsible for variations in prion disease phenotypes (prion strains). In this work, we use atomic force microscopy, FTIR spectroscopy and magic-angle spinning NMR to devise structural models of mouse prion protein fibrils prepared in three different denaturing conditions. We find that the fibril core region as well as the structure of its N- and C-terminal parts is almost identical between the three fibrils. In contrast, the central part differs in length of β-strands and the arrangement of charged residues. We propose that the denaturant ionic strength plays a major role in determining the structure of fibrils obtained in a particular condition by stabilizing fibril core interior-facing glutamic acid residues." @default.
• W3196857826 created "2021-09-13" @default.
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• W3196857826 date "2021-09-06" @default.
• W3196857826 modified "2023-09-27" @default.
• W3196857826 title "Aggregation Condition–Structure Relationship of Mouse Prion Protein Fibrils" @default.
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• W3196857826 doi "https://doi.org/10.3390/ijms22179635" @default.
• W3196857826 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8431800" @default.
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• W3196857826 hasPublicationYear "2021" @default.
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