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- W1996427183 abstract "Understanding the aggregation mechanism of amyloid fibrils and characterizing their structures are important steps in the investigation of several neurodegenerative disorders associated with the misfolding of proteins. We report a simulation study of coherent two-dimensional chiral signals of three NMR structures of Aβ protein fibrils associated with Alzheimer's Disease, two models for Aβ(8-40) peptide wild-type (WT) and one for the Iowa (D23N) Aβ(15-40) mutant. Both far-ultraviolet (FUV) signals (λ = 190-250 nm), which originate from the backbone nπ* and ππ* transitions, and near-ultraviolet (NUV) signals (λ ≥ 250 nm) associated with aromatic side chains (Phe and Tyr) show distinct cross-peak patterns that can serve as novel signatures for the secondary structure." @default.
- W1996427183 created "2016-06-24" @default.
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- W1996427183 date "2011-10-20" @default.
- W1996427183 modified "2023-10-16" @default.
- W1996427183 title "Distinguishing Amyloid Fibril Structures in Alzheimer’s Disease (AD) by Two-Dimensional Ultraviolet (2DUV) Spectroscopy" @default.
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- W1996427183 doi "https://doi.org/10.1021/bi201317c" @default.
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