Protein folding is a process in which a polypeptide is folded into a 3-dimensional conformation which is necessary for proper protein function. Failure to fold can produce inactive protein. A protein molecule folds during or after its biosynthesis.

The native conformation of a protein is determined by its amino acid sequences. This hypothesis was proved by an experiment, in which denaturation followed by renaturation folds the chain in its native structure.

Molten globule is a state in which interior side chains remain mobile, less compact and there is no proper packing. This state is completely different from the native and denatured state.

The ability of chaperones to synthesis in large amount after a brief exposure to elevated temperature(42°C) makes them heat shock protein(Hsp). Basically, the eukaryotic cell has two major families of chaperones called Hsp60 and Hsp70.

Hsp70 is induced by stress and these are the primary proteins which prevent polypeptide chain from misfolding and maintained it in an unfolded state. It also helps in translocation of the protein from the cytosol into ER or mitochondria.