Amyloid fibrils are associated with many fatal degenerative diseases of humans a

Question

Amyloid fibrils are associated with many fatal degenerative diseases of humans and livestock. Livestock diseases such as scrapie in sheep and bovine spongiform encephalitis (BSE, or mad cow disease) have major negative impacts on agriculture. Human diseases characterized by amyloid fibrils include Alzheimer's disease and Creutzfeldt-Jakob disease. The images below show a short segment of a typical amyloid fibril. The image on the left shows the side chains protruding from the faces of the beta-sheets. Choose the true statements about amyloid fibrils. Soluble proteins that misfold and form amyloid fibrils become insoluble. Proteins that convert to an amyloid fibril structure tend to have low solubility in their native form. Nucleation of amyloid structure may be triggered when two j3-sheet regions from two partially folded proteins associate. An amyloid fibril is stabilized by hydrophobic interactions between aromatic residues. An amyloid fibril typically forms from aggregates of misfolded peptides resulting from frameshift mutations.

Explanation / Answer

The following statements are true, from the above given, regarding the amyloid structure:

1. Amyloid fibres have high amount of beta sheet structure - true. (amyloid is defined as extracellular, proteinaceous deposits that have beta sheet structures).

3. Because most newly synthesised proteins fold correctly, the accumulation of misfold proteins tends to occur slowly, thus explaining the slow onset of disease. - true (Generally, newly synthesized proteins fold correctly. Hence, accumulation of misfolded proteins is too slow to have a quick onset.)

5. Proteins that form amyloid fibrils are normally soluble - true

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