Hydrogen bonds, disulphide linkages, van der Waals, and electrostatic forces stabilize the tertiary structure, representing the overall folding of polypeptide chains. The quaternary structure involves the spatial arrangement of subunits in proteins composed of two or more polypeptide chains.
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Tertiary structure of proteins is stabilized by a variety of forces, including hydrophobic interactions, hydrogen bonds, ionic bonds, and disulfide bridges. Hydrophobic interactions drive the folding of the polypeptide into a compact, three-dimensional structure, while hydrogen bonds and ionic interactions contribute to specific folding patterns. Disulfide bridges, covalent bonds between cysteine residues, add further stability. Quaternary structure involves the arrangement of multiple polypeptide subunits, and the forces stabilizing it include the same non-covalent interactions observed in tertiary structure, along with additional interactions between subunits, such as van der Waals forces and salt bridges, contributing to the overall stability and functionality of the protein complex.