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Aleksandr-060686 [28]
4 years ago
13

Proper folding of proteins is essential for their biological activity. In general, the functional conformation of a protein is t

he conformation with lowest energy. This means that if an unfolded protein is allowed to reach equilibrium, it should assemble automatically into its native, functioning folded state. Why then is there a need for molecular chaperones and chaperonins in cells?
Biology
1 answer:
romanna [79]4 years ago
6 0
<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

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