Abstract:Several proteins and peptides tend to form an amyloid fibril, causing a range of unrelated diseases, from neurodegenerative to certain types of cancer. In the native state, these proteins are folded and soluble. However, these proteins acquired β‐sheet amyloid fibril due to unfolding and aggregation. The conversion mechanism from well‐folded soluble into amorphous or amyloid fibril is not well understood yet. Here, we induced unfolding and aggregation of hen egg‐white lysozyme (HEWL) by reducing agent dithioth… Show more
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