Answer:
a. Amyloid fibrils have a high amount of β-sheet structure.
c. 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.
e. Proteins that form amyloid fibrils are normally soluble.
Explanation:
Amyloids can be defined as fibrillar protein aggregates composed of a β-sheet secondary structure. In general, the amyloid fibrils are composed by soluble proteins that are assembled to form insoluble resistant to degradation fibers. In humans, defective amyloid proteins produced by misfolding are known to produce diseases (amyloidosis) capable of altering the function of tissues and organs. Systemic forms of amyloidosis are common in neurodegenerative disorders.
Right and left pubic bodies
I think the answer would be protons
A similarity in both recrystallization and replacement modes of preservation is that delicate tissue and organs are not preserved.
<h3>What are recrystallization and replacement modes of preservation?</h3>
Recrystallization is a mode of preservation of fossils in which the internal structure of the fossils is changed by addition of more minerals to form larger crystal of the same material.
Replacement is a mode of preservation in which new material replaces the original material in the fossil.
In both methods of preservation, delicate tissue and organs are not preserved.
Therefore, a similarity in both recrystallization and replacement modes of preservation is that delicate tissue and organs are not preserved.
Learn more about fossils preservation at: brainly.com/question/2023023
#SPJ1
