Final answer:
The quaternary structure of a protein is primarily stabilized by hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide linkages, not by covalent bonds, making the statement false.
Step-by-step explanation:
The statement 'Covalent bonds are the most common types of bonds involved in holding the quaternary structure of a protein together' is false. While covalent bonds are indeed vital to protein structure, forming strong connections between atoms that do not dissociate in water, they are not the most common bonds in the quaternary level of protein structure.
Instead, the quaternary structure is stabilized by a variety of interactions including hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide linkages. It is these weaker interactions that play a more significant role in holding together the multiple subunits that form the quaternary structure of a protein. Although covalent bonds can contribute to quaternary structure, particularly through disulfide bonds, they are not the primary means of stabilization at this level.