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  • Title: Methods for Structural Analysis of Amyloid Fibrils in Misfolding Diseases.
    Author: Vadukul DM, Al-Hilaly YK, Serpell LC.
    Journal: Methods Mol Biol; 2019; 1873():109-122. PubMed ID: 30341606.
    Abstract:
    Many proteins and peptides are able to self-assemble in solution in vitro and in vivo to form amyloid-like fibrils. These fibrils share common structural characteristics. In order for a fibril to be characterized as amyloid, it is expected to fit certain criteria including the composition of cross-β. Here we describe how the formation of amyloid fibrils can be characterized in vitro using a variety of methods including circular dichroism and intrinsic tyrosine/tryptophan fluoresence to follow conformational changes; Thioflavin and/or ThS assembly to monitor nucleation and growth; transmission electron microscopy to visualize fibrillar morphology and X-ray fiber diffraction to examine cross-β structure.
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