<h2>Protein folding </h2>
Explanation:
- Molecular chaperones bind to nascent and folding or misfolded proteins (through improperly exposed hydrophobic regions) and stabilize the polypeptide so it can fold into its native state
- They have the ability to prevent non-specific aggregation by binding to non-native proteins
- They play an important role in protecting cells from being damaged under environmental stress, such as extreme heat, poisoning, or mental stress
- Most common chaperones are heat shock proteins which are also called stress proteins
- The intracellular folding environment for proteins is chaotic because of the presence of other biomolecules, folding proteins, improper or fluctuating pH, heat, and other denaturants
- Chaperonins provide actual chambers for misfolded proteins to properly refold, segregating the protein from the chaotic cellular environment.
- The main key function of chaperonins is to assist in the folding of large protein molecules
<span>Which structure secretes digestive enzymes that break down carbohydrates, fats, and proteins? A. Pancreas
Most of the enzyme in the intestinal system is made by pancreas. Pancreas will also secrete insulin to make cell utilize glucose. The Large intestine is absorbing water. Salivary glands mostly digest carbohydrate.</span>
Eyeglasses<span> (also called spectacles) are</span><span> the most common form of </span>eye wear.<span> They are used to correct or improve many types of vision problems. They are a frame that holds two pieces of glass or plastic, which have been ground into lenses to correct refractive errors.</span>
A predator kills and eats a prey animal.