Question

Choose the true statements about amyloid fibrils. 3 options are correct.

Answer 1

Answer:

Options 1, 3 and 4.

Because most newly synthesized proteins fold correctly, the accumulation of misfolded proteins (or fragments) tends to occur slowly, thus explaining the slow onset of disease.

An amyloid fibril is stabilized by hydrophobic interactions between aromatic residues.

4) Soluble proteins that misfold and form amyloid fibrils become insoluble.

Explanation:

Amloid fibrils are peptide or proteins that are formed during invivo or invitro conditions. They ate formed when soluble proteins combine together to for insoluble fibres that are resistant to degradation. They are found in extracellular tissues and posses pathological effect. They accumulate after nerve cells and causes several illness.

An amyloid fibril is stabilized by hydrophobic interactions between aromatic residues.

4) Soluble proteins that misfold and form amyloid fibrils become insoluble.

An amyloid fibril is stabilized by hydrophobic interactions between aromatic residues.

Soluble proteins that misfold and form amyloid fibrils become insoluble.

Answer 2

Answer:

The correct answers are options 1) "Because most newly synthesized proteins fold correctly, the accumulation of misfolded proteins (or fragments) tends to occur slowly, thus explaining the slow onset of disease". 3) "An amyloid fibril is stabilized by hydrophobic interactions between aromatic residues", and 4) "Soluble proteins that misfold and form amyloid fibrils become insoluble".

Explanation:

Amyloid fibrils are protein aggregates that can cause pathological conditions, for instance, they are found in brain tissue in people with Alzheimer disease. This disease, and other relates diseases, have a slow onset because most newly synthesized proteins fold correctly and the protein aggregates are made up misfolded proteins. This newly synthesized proteins are soluble, but once the proteins are misfolded, they form amyloid fibrils that are insoluble. The amyloid fibrils are stabilized by hydrophobic interactions between aromatic residues, which are formed within the complex of insoluble misfolded proteins.