Final answer:
Chaperonins, ubiquitin, and proteasomes are involved in the degradation of proteins.
Step-by-step explanation:
Proteins are degraded through a process involving chaperonins, ubiquitin, and proteasomes.
A chaperonin is a protein that assists in the folding of other proteins. It helps prevent misfolding and promotes proper folding, which is crucial for a protein's function.
Ubiquitin is a small protein that marks damaged or unwanted proteins for degradation. It attaches itself to the target protein and directs it to a proteasome.
A proteasome is a large complex of proteins that degrades the targeted proteins marked by ubiquitin. It breaks down the proteins into smaller peptides, which can be further processed or recycled.
In summary, all of the options listed (chaperonin, ubiquitin, and proteasome) play a role in the degradation of proteins.