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: -The tertiary structure of a protein consists of the way a polypeptide is formed of a complex molecular shape. This is caused by R-group interactions such as ionic and hydrogen bonds, disulphide bridges, and hydrophobic & hydrophilic interactions.

Detailed explanation-3: -Four interactions stabilize the tertiary structure of a protein: (a) ionic bonding, (b) hydrogen bonding, (c) disulfide linkages, and (d) dispersion forces. When a protein contains more than one polypeptide chain, each chain is called a subunit.

Detailed explanation-4: -The bonds that provide stabilisation to the tertiary structure of the protein are disulphide bonds, ionic bonds and hydrophobic bonds and wander Waal’s interactions. Myoglobin is an example of the tertiary structure of the protein.

Detailed explanation-5: -Whereas hydrogen-bonding interactions between backbone atoms stabilize secondary structure, ionic interactions, hydrogen bonds, and van der Waals interactions help stabilize tertiary and quaternary structure.