Methods for structural analysis of amyloid fibrils in misfolding diseases

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

Full text not available from this repository.

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://sro.sussex.ac.uk/id/eprint/80066
📧 Request an update