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- W4308001686 abstract "Using amylin(20-29) as a model system, we demonstrate that Raman spectroscopy can be used to determine the molecular structure of amyloid fibrils. We use polarized Raman spectroscopy measurements and the conformationally-sensitive Amide III3 mode to determine the distributions of peptide backbone amide C=O and CN bond orientations, as well as Ramachandran Psi dihedral angles, adopted by amylin(20-29) fibrils. We use these experimentally measured distributions as structural constraints to guide molecular dynamics (MD) simulations of an amylin(20-29) fibril structure. Our model indicates that amylin(20-29) fibrils adopt an antiparallel beta-sheet cross-beta core structure in excellent agreement with previous studies. Overall, our results show that Raman spectroscopy provides high-resolution structural information about amyloid fibrils that complements gold standard techniques such as solid-state NMR and cryogenic electron microscopy. We anticipate that the Raman methods developed here will aide in determining detailed structural models of amyloid fibrils directly in physiologically relevant systems such as biological tissue and cell cultures." @default.
- W4308001686 created "2022-11-07" @default.
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- W4308001686 date "2022-11-02" @default.
- W4308001686 modified "2023-09-29" @default.
- W4308001686 title "Towards Determining Amyloid Fibril Structures Using Experimental Constraints from Raman Spectroscopy" @default.
- W4308001686 doi "https://doi.org/10.26434/chemrxiv-2022-zrzmf-v2" @default.
- W4308001686 hasPublicationYear "2022" @default.
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