BIOMOLECULES AND ENZYMES

Detailed explanation-1: -During the denaturation of proteins, the secondary and tertiary structures get destroyed and only the primary structure is retained. Covalent bonds are broken and interaction between amino-acid chains gets disrupted. This results in the loss of biological activity of the proteins.

Detailed explanation-2: -A protein becomes denatured when its normal shape gets deformed because some of the hydrogen bonds are broken. Weak hydrogen bonds break when too much heat is applied or when they are exposed to an acid (like citric acid from lemon juice).

Detailed explanation-3: -Denaturation breaks the intramolecular bonds, such as hydrogen bonds and van der Waals interactions, that hold the protein in its three-dimensional shape.

Detailed explanation-4: -When a solution of a protein is boiled, the protein frequently becomes insoluble-i.e., it is denatured-and remains insoluble even when the solution is cooled. The denaturation of the proteins of egg white by heat-as when boiling an egg-is an example of irreversible denaturation.

Detailed explanation-5: -When a protein is denatured, secondary and tertiary structures are altered but the peptide bonds of the primary structure between the amino acids are left intact. Since all structural levels of the protein determine its function, the protein can no longer perform its function once it has been denatured.