BIOMOLECULES AND ENZYMES

Detailed explanation-1: -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-2: -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-3: -The R group determines the characteristics (size, polarity, and pH) for each type of amino acid. Peptide bonds form between the carboxyl group of one amino acid and the amino group of another through dehydration synthesis. A chain of amino acids is a polypeptide.

Detailed explanation-4: -Primarily, the interactions among R groups creates the complex three-dimensional tertiary structure of a protein. The nature of the R groups found in the amino acids involved can counteract the formation of the hydrogen bonds described for standard secondary structures such as the alpha helix.