ArticleProtein science : a publication of the Protein Society2009
Differential stability of the bovine prion protein upon urea unfolding.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 32 citations in OpenAlex.
- Prion-derived tetrapeptide stabilizes thermolabile insulin via conformational trapping.iScience · 2021Article
- A novel Gerstmann-Sträussler-Scheinker disease mutation defines a precursor for amyloidogenic 8 kDa PrP fragments and reveals N-terminal structural changes shared by other GSS alleles.PLoS pathogens · 2018Article
- Recombinant PrP and Its Contribution to Research on Transmissible Spongiform Encephalopathies.Pathogens (Basel, Switzerland) · 2017Review
- How cooperative are protein folding and unfolding transitions?Protein science : a publication of the Protein Society · 2016Review
- Molecular dynamics simulations capture the misfolding of the bovine prion protein at acidic pH.Biomolecules · 2014Article
- Thermodynamic characterization of the unfolding of the prion protein.Biophysical journal · 2014Article
- N-terminal helix-cap in α-helix 2 modulates β-state misfolding in rabbit and hamster prion proteins.PloS one · 2013Article
- Energy landscape analysis of native folding of the prion protein yields the diffusion constant, transition path time, and rates.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding.Journal of molecular biology · 2010Article
- Prion fibrillization is mediated by a native structural element that comprises helices H2 and H3.The Journal of biological chemistry · 2010Article
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Authors and funding
5 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Prion diseases, or transmissible spongiform encephalopathies, are a group of infectious neurological diseases associated with the structural conversion of an endogenous protein (PrP) in the central nervous system. There are two major forms of this protein: the native and noninfectious cellular form, PrP(C); and the misfolded, infectious, and proteinase K-resistant form, PrP(Sc). The C-terminal domain of PrP(C) is mainly alpha-helical in structure, whereas PrP(Sc) in known to aggregate into an assembly of beta-sheets, forming amyloid fibrils. To identify the regions of PrP(C) potentially involved in the initial steps of the conversion to the infectious conformation, we have used high-resolution NMR spectroscopy to characterize the stability and structure of bovine recombinant PrP(C) (residues 121 to 230) during unfolding with the denaturant urea. Analysis of the 800 MHz (1)H NMR spectra reveals region-specific information about the structural changes occurring upon unfolding. Our data suggest that the dissociation of the native beta-sheet of PrP(C) is a primary step in the urea-induced unfolding process, while strong hydrophobic interactions between helices alpha1 and alpha3, and between alpha2 and alpha3, stabilize these regions even at very high concentrations of urea.
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