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• W2013157094 startingPage "e94469" @default.
• W2013157094 abstract "Prion protein is known to have the ability to adopt a pathogenic conformation, which seems to be the basis for protein-only infectivity. The infectivity is based on self-replication of this pathogenic prion structure. One of possible mechanisms for such replication is the elongation of amyloid-like fibrils. We measured elongation kinetics and thermodynamics of mouse prion amyloid-like fibrils at different guanidine hydrochloride (GuHCl) concentrations. Our data show that both increases in temperature and GuHCl concentration help unfold monomeric protein and thus accelerate elongation. Once the monomers are unfolded, further increases in temperature raise the rate of elongation, whereas the addition of GuHCl decreases it. We demonstrated a possible way to determine different activation energies of amyloid-like fibril elongation by using folded and unfolded protein molecules. This approach separates thermodynamic data for fibril-assisted monomer unfolding and for refolding and formation of amyloid-like structure." @default.
• W2013157094 created "2016-06-24" @default.
• W2013157094 creator A5000531071 @default.
• W2013157094 creator A5072233491 @default.
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• W2013157094 date "2014-04-18" @default.
• W2013157094 modified "2023-09-26" @default.
• W2013157094 title "Elongation of Mouse Prion Protein Amyloid-Like Fibrils: Effect of Temperature and Denaturant Concentration" @default.
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• W2013157094 doi "https://doi.org/10.1371/journal.pone.0094469" @default.
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