Abstract
Elucidation of the underlying core structure of amyloid fibrils is essential for understanding the mechanism by which amyloid fibrils are formed and deposited. Conventional methods of X-ray crystallography and NMR cannot be used, since the fibers are insoluble and heterogeneous. X-ray fiber diffraction is one method that has been successfully used to examine the structure of these insoluble fibers. The procedure involves the formation of suitable, ordered amyloid fibrils and characterization (by electron microscopy), partial alignment of fibers, X-ray data collection, data analysis, and finally, model building.
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Makin, O.S., Serpell, L.C. (2005). X-Ray Diffraction Studies of Amyloid Structure. In: Sigurdsson, E.M. (eds) Amyloid Proteins. Methods in Molecular Biology™, vol 299. Humana Press. https://doi.org/10.1385/1-59259-874-9:067
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DOI: https://doi.org/10.1385/1-59259-874-9:067
Publisher Name: Humana Press
Print ISBN: 978-1-58829-337-4
Online ISBN: 978-1-59259-874-8
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