Protein aggregation and amyloidogenesis are closely associated with the
pathogenesis of neurodegenerative diseases. Elucidating the morphology and structure
of the amyloid aggregates or fibrils is important for understanding the molecular
mechanisms of these proteinopathies. This review article describes the general
principle and establishment of solid-state circular dichroism (ssCD) spectroscopy,
and discusses its application for the analysis of secondary structures of proteins or
peptides in amyloids and structural transformation of these proteins or peptides during
their amyloidogenic aggregation.
Keywords: Circular dichroism, Solid state, Protein amyloid, Secondary structure, Structural transformation.
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