<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
Answer:
The greater the surface-area to volume ratio of a cell, the easier it is for the cell to get rid of wastes and take in essential materials such as oxygen and nutrients.
Hope this helps!
Answer:
the upper partwas full of water an
I have the answer! Click the link below to find it.
www.//easel.teachers pays.com