Question

Explain denaturation of protein with an example.

Answer 1

Hint: The loss of the quaternary, tertiary or secondary structure of a protein molecule due to the application of an external stress or energy is known as denaturation. Whenever we boil an egg, the yellow liquid yolk solidifies due to the denaturation process.

Complete step by step answer:
Denaturation is a process in which proteins or nucleic acids lose the quaternary structure, tertiary structure and secondary structure which is present in their native state by the application of some external stress or compound such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), radiation or heat. Denatured proteins can exhibit a wide range of characteristics, from conformational change and loss of solubility to aggregation due to the exposure of hydrophobic groups. Protein denaturation is also a consequence of cell death. If proteins in a living cell are denatured, this results in disruption of cell activity and possibly cell death. Denatured proteins lose their 3D structure and therefore cannot function.
The protein molecule is present initially in the globular form and on the application of an external stress/force, it starts unwinding and there is a breakage of the bonds which used to bind them in their globular form.
Example-One must have observed the hardening of the yellow fluid part in the egg when it is subjected to a boiling temperature. Here, the temperature acts as an external stress and breaks the bonds in the proteins and helps the albumin and the central protein part to change its structure and get solidified.

Note:
Denaturation involves the breaking of many of the weak linkages, or bonds (e.g. hydrogen bonds), within a protein molecule that is responsible for the highly ordered structure of the protein in its natural (native) state. Denatured proteins have a looser, more random structure; most are insoluble.