The native helical structure of protein is lost.

The primary structure of a protein with peptide linkages remains intact; that is, peptide bonds are not hydrolysed.

Protein loses its biological activity.

Denaturated protein becomes insoluble in the solvent in which it was originally soluble.

The viscosity of denaturated protein is increased.

Denaturation is associated with increase in ionizable and sulfhydryl groups of protein. This is due to loss of hydrogen and disulphide bonds.

Denaturated protein is more easily digested, that is, due to increased exposure of peptide bonds to the enzyme.

Cooking causes protein denaturation and, therefore, more easily digested.

Denaturation is usually irreversible.

Example: Omelet can be prepared from an egg, which is irreversible.

Careful denaturation is sometimes reversible, which is known as renaturation.

Example: Hb undergoes denaturation in the presence of salicylates by removing salicylates; Hb is renaturated.

Denaturated protein is not crystallised.