Choose the true statements about amyloid fibrils. Proteins that form amyloid fibrils are normally soluble. Proteins that convert to an amyloid structure form soluble fibrils. Nucleation of amyloid structure may be triggered when two ?-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.
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Proteins that form amyloid fibrils are normally soluble: This statement is true. Proteins that form amyloid fibrils are usually soluble under normal conditions, but they can aggregate and form insoluble fibrils under certain circumstances. Show more…
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Choose the true statements about amyloid fibrils: An amyloid fibril typically forms from aggregates of misfolded peptides resulting from frameshift mutations. Proteins that convert to an amyloid fibril structure tend to have low solubility in their native form. An amyloid fibril is stabilized by hydrophobic interactions between aromatic residues. Nucleation of amyloid structure may be triggered when two ̠-sheet regions from two partially folded proteins associate. Soluble proteins that misfold and form amyloid fibrils become insoluble.
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Choose the true statements about amyloid fibrils. Proteins that convert to an amyloid structure form soluble fibrils. Amyloid fibrils have a high amount of ̑-helical structure. Nucleation of amyloid structure may be triggered when two ̒-sheet regions from two partially folded proteins associate. Proteins that form amyloid fibrils are normally soluble. Some amyloid fibrils are formed from proteolytic fragments that self-assemble into extended ̒-sheet structures.
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Choose the true statements about amyloid fibrils. Three options are correct. 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. 2) An amyloid fibril typically forms from aggregates of misfolded peptides resulting from frameshift mutations. 3) An amyloid fibril is stabilized by hydrophobic interactions between aromatic residues. 4) Soluble proteins that misfold and form amyloid fibrils become insoluble. 5) Proteins that convert to an amyloid fibril structure tend to have low solubility in their native form.
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