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Nanoscale Imaging and Characterisation of Amyloid- (Hardcover, 1st ed. 2016): Claire Louisa Tinker-Mill Nanoscale Imaging and Characterisation of Amyloid- (Hardcover, 1st ed. 2016)
Claire Louisa Tinker-Mill
R3,467 Discovery Miles 34 670 Ships in 12 - 19 working days

This thesis presents a method for reliably and robustly producing samples of amyloid- (A ) by capturing them at various stages of aggregation, as well as the results of subsequent imaging with various atomic force microscopy (AFM) methods, all of which add value to the data gathered by collecting information on the peptide's nanomechanical, elastic, thermal or spectroscopical properties. Amyloid- (A ) undergoes a hierarchy of aggregation following a structural transition, making it an ideal subject of study using scanning probe microscopy (SPM), dynamic light scattering (DLS) and other physical techniques. By imaging samples of A with Ultrasonic Force Microscopy, a detailed substructure to the morphology is revealed, which correlates well with the most advanced cryo-EM work. Early stage work in the area of thermal and spectroscopical AFM is also presented, and indicates the promise these techniques may hold for imaging sensitive and complex biological materials. This thesis demonstrates that physical techniques can be highly complementary when studying the aggregation of amyloid peptides, and allow the detection of subtle differences in their aggregation processes.

Nanoscale Imaging and Characterisation of Amyloid- (Paperback, Softcover reprint of the original 1st ed. 2016): Claire Louisa... Nanoscale Imaging and Characterisation of Amyloid- (Paperback, Softcover reprint of the original 1st ed. 2016)
Claire Louisa Tinker-Mill
R3,315 Discovery Miles 33 150 Ships in 10 - 15 working days

This thesis presents a method for reliably and robustly producing samples of amyloid- (A ) by capturing them at various stages of aggregation, as well as the results of subsequent imaging with various atomic force microscopy (AFM) methods, all of which add value to the data gathered by collecting information on the peptide's nanomechanical, elastic, thermal or spectroscopical properties. Amyloid- (A ) undergoes a hierarchy of aggregation following a structural transition, making it an ideal subject of study using scanning probe microscopy (SPM), dynamic light scattering (DLS) and other physical techniques. By imaging samples of A with Ultrasonic Force Microscopy, a detailed substructure to the morphology is revealed, which correlates well with the most advanced cryo-EM work. Early stage work in the area of thermal and spectroscopical AFM is also presented, and indicates the promise these techniques may hold for imaging sensitive and complex biological materials. This thesis demonstrates that physical techniques can be highly complementary when studying the aggregation of amyloid peptides, and allow the detection of subtle differences in their aggregation processes.

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