Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.707793
Title: Aggregation of alpha-synuclein using single-molecule spectroscopy
Author: Iljina, Marija
ISNI:       0000 0004 6057 0515
Awarding Body: University of Cambridge
Current Institution: University of Cambridge
Date of Award: 2017
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Abstract:
The aggregation of alpha-synuclein (αS) protein from soluble monomer into solid amyloid fibrils in the brain is associated with a range of devastating neurodegenerative disorders such as Parkinson’s disease. Soluble oligomers formed during the aggregation process are highly neurotoxic and are thought to play a key role in the onset and spreading of disease. Despite their importance, these species are difficult to study by conventional experimental approaches owing to their transient nature, heterogeneity, low abundance and a remarkable sensitivity of the oligomerisation process to the chosen experimental conditions. In this thesis, well-established single-molecule techniques have been utilised to study the aggregation and oligomerisation of αS in solution.
Supervisor: Not available Sponsor: Christs College Cambridge
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.707793  DOI:
Keywords: alpha-synuclein ; single-molecule FRET ; protein aggregation ; neurodegeneration
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