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- W2935864073 endingPage "574" @default.
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- W2935864073 abstract "Molecular level insight into the interplay between protein sequence, structure, and conformational dynamics is crucial for the comprehensive understanding of protein folding, misfolding, and aggregation phenomena that are pertinent to the formation of amyloid fibrils implicated in several degenerative diseases. Computational modelling provides insight into protein behaviour at spatial and temporal resolution still largely outside the reach of experiments. Herein we present an account of our theoretical modelling research conducted in collaboration with several experimental groups where we explored the effects of local environment on the structure and aggregation propensity of several types of amyloidogenic peptides and proteins, including apolipoprotein C-II, insulin, amylin, and amyloid-β using a variety of computational approaches." @default.
- W2935864073 created "2019-04-25" @default.
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- W2935864073 creator A5063020733 @default.
- W2935864073 date "2019-01-01" @default.
- W2935864073 modified "2023-10-18" @default.
- W2935864073 title "The Enigma of Amyloid Forming Proteins: Insights From Molecular Simulations" @default.
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- W2935864073 doi "https://doi.org/10.1071/ch19059" @default.
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