- Molecular chaperone proteins primarily assist in the proper folding of nascent or stress-denatured proteins, ensuring they attain their correct three-dimensional structure.
- They also prevent aggregation of misfolded proteins, which can be toxic to cells.
- Unlike enzymes that catalyze reactions, chaperones do not form covalent bonds but stabilize folding intermediates.
- This function is crucial for maintaining cellular protein homeostasis and preventing diseases linked to protein misfolding.