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• W2022793853 endingPage "311" @default.
• W2022793853 startingPage "303" @default.
• W2022793853 abstract "The role of β-sheets in the early stages of protein aggregation, specifically amyloid formation, remains unclear. Interpretations of kinetic data have led to a specific model for the role of β-sheets in polyglutamine aggregation. According to this model, monomeric polyglutamine, which is intrinsically disordered, goes through a rare conversion into an ordered, metastable, β-sheeted state that nucleates aggregation. It has also been proposed that the probability of forming the critical nucleus, a specific β-sheet conformation for the monomer, increases with increasing chain length. Here, we test this model using molecular simulations. We quantified free energy profiles in terms of β-content for monomeric polyglutamine as a function of chain length. In accord with estimates from experimental data, the free energy penalties for forming β-rich states are in the 10–20 kcal/mol range. However, the length dependence of these free energy penalties does not mirror interpretations of kinetic data. In addition, although homodimerization of disordered molecules is spontaneous, the imposition of conformational restraints on polyglutamine molecules does not enhance the spontaneity of intermolecular associations. Our data lead to the proposal that β-sheet formation is an attribute of peptide-rich phases such as high molecular weight aggregates rather than monomers or oligomers." @default.
• W2022793853 created "2016-06-24" @default.
• W2022793853 creator A5024363437 @default.
• W2022793853 creator A5030276329 @default.
• W2022793853 creator A5084455783 @default.
• W2022793853 date "2009-07-01" @default.
• W2022793853 modified "2023-10-09" @default.
• W2022793853 title "Thermodynamics of β-Sheet Formation in Polyglutamine" @default.
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• W2022793853 doi "https://doi.org/10.1016/j.bpj.2009.05.003" @default.
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