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.

Detailed explanation-2: -R group interactions that contribute to tertiary structure include hydrogen bonding, ionic bonding, dipole-dipole interactions, and London dispersion forces – basically, the whole gamut of non-covalent bonds.

Detailed explanation-3: -Tertiary structure is formed by the folding of the secondary structure sheets or helices into one another. The tertiary structure of protein is the geometric shape of the protein. It usually has a polypeptide chain as a backbone, with one or more secondary structures.

Detailed explanation-4: -The tertiary structure is the protein folded into its precise 3D structure, relating to the functon. This is held together by a range of non-covelant interactions between side groups, including ionic interations, disuplhide bridges, hydrophobic interactions, Van der Waals forces and hydrogen bonds.