The tertiary and secondary structures of proteins differ in their stability due to various types of bonding interactions. Secondary structure stability is primarily dependent on hydrogen bonding, while tertiary structure stability involves multiple bonding interactions including hydrophobic, ionic, and disulfide bondings.
Tertiary structure of a protein is the unique three-dimensional shape determined by chemical interactions between amino acid side chains, leading to a specific organized shape. Quaternary structure involves multiple folded polypeptides called subunits. The stability of secondary structure in a protein relies primarily on hydrogen bonding, while tertiary structure is maintained by hydrophobic interactions, ionic bonding, hydrogen bonding, and disulfide linkages.
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