Amyloid formation due to altered protein folding and aggregation has gained significant attention due to its association with neurodegenerative disorders such as Alzheimer's disease, Parkinson's disease, Huntington's disease, and systemic lysozyme amyloidosis. Amyloids are characterized by parallel and anti-parallel cross-β-strands arranged to form stacks of sheets that provide stability and rigidity to the amyloid core. The prototypic protein Hen Egg White Lysozyme (HEWL) has been extensively used to understand protein hydrolysis, fragmentation, folding, misfolding, and amyloid formation.
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