BIOMOLECULES AND ENZYMES

Detailed explanation-1: -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.

Detailed explanation-2: -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-3: -Folded proteins are stabilized by thousands of noncovalent bonds between amino acids. In addition, chemical forces between a protein and its immediate environment contribute to protein shape and stability.

Detailed explanation-4: -Intra-and Intermolecular interactions help to stabilize Tertiary and Quaternary Structure. 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.

Detailed explanation-5: -The tertiary structure is primarily due to interactions between the R groups of the amino acids that make up the protein.