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• W2000679811 startingPage "6324" @default.
• W2000679811 abstract "Understanding fibrillogenesis at a molecular level requires detailed structural characterization of amyloid fibrils. The combination of deep UV resonance Raman (DUVRR) spectroscopy and post mortem hydrogen−deuterium exchange (HX) was utilized for probing parallel vs antiparallel β-sheets in fibrils prepared from full-length Aβ1−40 and Aβ34−42 peptides, respectively. Using previously published structural data based on solid-state NMR analysis, we verified the applicability of Asher’s approach for the quantitative characterization of peptide conformation in the Aβ1−40 fibril core. We found that the conformation of the parallel β-sheet in the Aβ1−40 fibril core is atypical for globular proteins, while in contrast, the antiparallel β-sheet in Aβ32−42 fibrils is a common structure in globular proteins. In contrast to the case for globular proteins, the conformations of parallel and antiparallel β-sheets in Aβ fibril cores are substantially different, and their differences can be distinguished by DUVRR spectroscopy." @default.
• W2000679811 created "2016-06-24" @default.
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• W2000679811 date "2010-04-20" @default.
• W2000679811 modified "2023-09-26" @default.
• W2000679811 title "Structural Variations in the Cross-β Core of Amyloid β Fibrils Revealed by Deep UV Resonance Raman Spectroscopy" @default.
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• W2000679811 doi "https://doi.org/10.1021/ja909074j" @default.
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