In large proteins such as myoglobin and enzymes, peptide chains are much looped, twisted and folded back on themselves to form a tertiary structure. Which bonds are involved in the formation of tertiary structure of proteins?

Step-by-step solution

The tertiary structure of proteins represents the overall three-dimensional folding of the polypeptide chain. This structure is stabilized by various non-covalent interactions, including hydrogen bonds, ionic bonds, van der Waals forces, and hydrophobic interactions. While disulphide bonds (covalent linkages) can also stabilize the tertiary structure in some proteins, myoglobin is a classic example of a globular protein that completely lacks disulphide bonds. Its tertiary structure is stabilized entirely by non-cov