BIOMOLECULES AND ENZYMES

Detailed explanation-1: -Denaturation involves the breaking of many of the weak linkages, or bonds (e.g., hydrogen bonds), within a protein molecule that are 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.

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 covalent bonds that hold the protein in its three-dimensional shape. Without the proper shape, the protein cannot function. Denaturation destroys the primary structure of the protein, and the protein breaks down to monomers.

Detailed explanation-4: -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-5: -Denaturation refers to the physical changes that take place in a protein exposed to abnormal conditions in the environment. Heat, acid, high salt concentrations, alcohol, and mechanical agitation can cause proteins to denature.