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Nanoscale Imaging and Characterisation of Amyloid-¿

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135,50 
Įprasta kaina: 169,38 
-20% su kodu: BOOKS
Kupono kodas: BOOKS
Akcija baigiasi: 2025-03-09
-20% su kodu: BOOKS
135,50 
Įprasta kaina: 169,38 
-20% su kodu: BOOKS
Kupono kodas: BOOKS
Akcija baigiasi: 2025-03-09
-20% su kodu: BOOKS
2025-02-28 169.3800 InStock
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Knygos aprašymas

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.

Informacija

Autorius: Claire Louisa Tinker-Mill
Serija: Springer Theses
Leidėjas: Springer Nature Switzerland
Išleidimo metai: 2016
Knygos puslapių skaičius: 172
ISBN-10: 3319395335
ISBN-13: 9783319395333
Formatas: 241 x 160 x 16 mm. Knyga kietu viršeliu
Kalba: Anglų

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