Vadukul, Devekee M, Al-Hilaly, Youssra K and Serpell, Louise C (2018) Methods for structural analysis of amyloid fibrils in misfolding diseases. In: Gomes, Cláudio M (ed.) Protein misfolding diseases. Humana Press, New York, NY, pp. 109-122. ISBN 9781493988198

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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.

Item Type:	Book Section
Schools and Departments:	School of Life Sciences > Biochemistry
Research Centres and Groups:	Dementia Research Group
Depositing User:	Youssra Al-Hilaly
Date Deposited:	09 Nov 2018 11:04
Last Modified:	09 Nov 2018 11:04
URI:	http://srodev.sussex.ac.uk/id/eprint/80066

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