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The polymorphic nature of amyloid assembly: Exploring fibril morphology and the structural relationship towards mechanical stability

Blakeman, Ben (2017) The polymorphic nature of amyloid assembly: Exploring fibril morphology and the structural relationship towards mechanical stability. Doctor of Philosophy (PhD) thesis, University of Kent,. (KAR id:66049)

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Abstract

The polymorphic nature of amyloid fibrils is important in the understanding of structural

progression. The work reported here uses Atomic force microscopy (AFM) to enhance

and stability towards breakage. A novel quantitative cluster analysis was developed

fibrils formed from three peptide sequences identified by the WALTZ algorithm, we have

structural models to predict the likely filament arrangements accessible to each. The

persistence length values for each respective population. These mechanical differences

subsequent image analysis.

amyloid fibrils formed in vitro and those formed in situ using a synthetic biology

similarities between fibrils formed using this system and those formed in vitro is of great

expands on possible fibril morphologies and the related mechanical properties, which

utilisation of amyloid fibrils in a biotechnology role.

Item Type: Thesis (Doctor of Philosophy (PhD))
Thesis advisor: Xue, Wei-Feng
Thesis advisor: Serpell, Louise
Uncontrolled keywords: Biochemistry, Biophysics, Amyloid, Atomic force microscopy, Protein, Structure, Fibril, Hierarchical clustering, Matlab
Divisions: Faculties > Sciences > School of Biosciences
SWORD Depositor: System Moodle
Depositing User: System Moodle
Date Deposited: 16 Feb 2018 15:10 UTC
Last Modified: 01 Jun 2020 23:00 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/66049 (The current URI for this page, for reference purposes)
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