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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Vadukul, D.M., Al-Hilaly, Y.K., Serpell, L.C. (2019). Methods for Structural Analysis of Amyloid Fibrils in Misfolding Diseases. In: Gomes, C. (eds) Protein Misfolding Diseases. Methods in Molecular Biology, vol 1873. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-8820-4_7
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DOI: https://doi.org/10.1007/978-1-4939-8820-4_7
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