AP BIOLOGY

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: -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.

Detailed explanation-4: -Within a protein, multiple amino acids are linked together by peptide bonds, thereby forming a long chain. Peptide bonds are formed by a biochemical reaction that extracts a water molecule as it joins the amino group of one amino acid to the carboxyl group of a neighboring amino acid.