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• W2153252106 abstract "Significance This study leverages a predictive protein-folding simulation model to study the free energy landscapes of fused oligomeric constructs to quantify the conditions under which these constructs spontaneously misfold. Constructs of this type have been used to probe the early stages of aggregation in the laboratory. Oligomeric species may be the toxic agents in misfolding-related diseases. The critical structures that initiate aggregation are shown to depend on specific sequence signals and thermodynamic conditions. Our results also suggest that branching due to the presence of multiple amyloidogenic segments may determine the morphology of protein aggregates." @default.
• W2153252106 created "2016-06-24" @default.
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• W2153252106 date "2013-11-27" @default.
• W2153252106 modified "2023-10-16" @default.
• W2153252106 title "Free energy landscapes for initiation and branching of protein aggregation" @default.
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• W2153252106 doi "https://doi.org/10.1073/pnas.1320483110" @default.
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