Final answer:
The chaperonin protein assists in protein folding by preventing aggregation and allowing polypeptide chains to properly form the critical tertiary structure with hydrophobic amino acids inside and hydrophilic on the surface.
Step-by-step explanation:
The chaperonin protein mentioned in the question is a molecular machine important for ensuring proper protein folding. This protein folding is crucial for the biological function of the protein. Chaperonins form a double ring tetradecamer structure, which is cylinder-shaped, that temporarily isolates the polypeptide to prevent aggregation and allows it to fold correctly. The hydrophobic amino acids tend to be tucked inside the final folded protein, with the hydrophilic amino acids exposed to the aqueous environment. This forms the tertiary structure of proteins, which may include motifs such as beta-pleated sheets and is maintained by various types of bonds and interactions between amino acid side chains.