The quaternary structure of proteins is stabilized by noncovalent bonds between complementary surface hydrophobic and hydrophilic regions on the polypeptide subunits, additionally, acidic and basic side chains can form salt linkages.
The arrangement of proteins and protein subunits in three-dimensional complexes or quaternary structures is stabilized and guided by multiple non-covalent interactions.
The two most common quaternary structures of multisubunit proteins are α-helices in globular proteins and β-sheets in fibrous proteins.
The functional properties of multi-subunit proteins depend on the quaternary structure.