How do molecular chaperones affect protein folding?

Molecular chaperones play a critical role in protein folding by assisting newly synthesized polypeptide chains in achieving their correct three-dimensional structure. Proteins need to fold into specific shapes to function properly, and sometimes they can misfold due to various factors including cellular stress or high concentrations of proteins. Molecular chaperones interact with these nascent polypeptides, preventing inappropriate interactions that could lead to misfolding or aggregation.

These chaperones do not provide the energy for the folding process nor do they break down misfolded proteins; rather, they facilitate and stabilize the folding process as it occurs. They may also assist in the refolding of proteins that have begun to misfold. By binding to the polypeptides at various stages of synthesis and folding, molecular chaperones effectively ensure that the protein adopts its correct conformation, which is essential for its function in the cell.