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: -Denaturation is a process in which proteins lose their shape and, therefore, their function because of changes in pH or temperature.

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: -Denaturation, such as the process of boiling an egg, causes a major phase change in proteins. Protein denaturation involves structural or conformational changes from the native structure without alteration of the amino acid sequence.

Detailed explanation-5: -As a result of denaturation, globules get unfolded and helixes get uncoiled. Secondary and tertiary structures of protein are destroyed, but the primary structures remain unaltered. It can be said that during denaturation, secondary and tertiary-structured proteins get converted into primary-structured proteins.