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Methods for structural analysis of amyloid fibrils in misfolding diseases
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posted on 2023-06-09, 15:47 authored by Devekee M Vadukul, Youssra Al-Hilaly, Louise SerpellLouise SerpellMany 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-ß. 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-ß structure.
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Publication status
- Published
Publisher
Humana PressExternal DOI
Volume
1873Page range
109-122Book title
Protein misfolding diseasesPlace of publication
New York, NYISBN
9781493988198Department affiliated with
- Biochemistry Publications
Research groups affiliated with
- Dementia Research Group Publications
Full text available
- No
Peer reviewed?
- Yes
Editors
Cláudio M GomesLegacy Posted Date
2018-11-09First Compliant Deposit (FCD) Date
2018-11-07Usage metrics
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