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• W2024748787 abstract "We studied the oligomerization of Alzheimer amyloid beta peptide (Aβ) using a replica exchange molecular dynamics (REMD) simulation. The simulation was performed with Aβ10-35 dimers, trimers, and tetramers. Extensive REMD simulations illustrated several possible oligomer conformations. As the size of the oligomer increased from a dimer to a tetramer, the number of possible configurations was reduced. We identified all the possible conformations for each oligomer and characterized their temperature dependence. It was found that the detailed structures of the oligomers, which may act as folding intermediates, are highly sensitive to the parameters of the simulation environment such as temperature and concentration. Structural diversities of Aβ oligomers suggest multiple pathways of the aggregation process." @default.
• W2024748787 created "2016-06-24" @default.
• W2024748787 creator A5046653471 @default.
• W2024748787 creator A5076338860 @default.
• W2024748787 date "2008-02-28" @default.
• W2024748787 modified "2023-09-29" @default.
• W2024748787 title "Computational Study on the Structural Diversity of Amyloid Beta Peptide (Aβ₁₀_-₃₅) Oligomers" @default.
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• W2024748787 doi "https://doi.org/10.1021/jp076450w" @default.
• W2024748787 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18303879" @default.
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