BIOMOLECULES AND ENZYMES

Detailed explanation-1: -The tertiary structure of a protein refers to the overall three-dimensional arrangement of its polypeptide chain in space. It is generally stabilized by outside polar hydrophilic hydrogen and ionic bond interactions, and internal hydrophobic interactions between nonpolar amino acid side chains (Fig. 4-7).

Detailed explanation-2: -Tertiary structure refers to the overall folding of the entire polypeptide chain into a specific 3D shape. The tertiary structure of enzymes is often a compact, globular shape.

Detailed explanation-3: -The tertiary structure of a protein describes the manner in which the secondary structural elements are arranged in three dimensions to create a stable molecular entity. In many cases it is convenient to describe a protein in terms of regions of the polypeptide chain that might fold autonomously.

Detailed explanation-4: -The structure of protein sets the foundation for its interaction with other molecules in the body and, therefore, determines its function.

Detailed explanation-5: -Hydrophobic Interactions These non-covalent bonds are the most important factor and driving force in the formation of the tertiary structure. If we place hydrophobic (water-hating) molecules in water, these molecules will aggregate together and form large chunks of hydrophobic molecules.