Final answer:
Peptides contain covalent disulfide bonds and hydrogen as well as ionic bonds in addition to peptide bonds. These interactions are crucial for maintaining peptide structure and function.
Step-by-step explanation:
Besides peptide bonds, other covalent bonds commonly found in peptides include disulfide bonds and, less commonly, ether bonds (in modified amino acids or side chain interactions). However, peptides also feature non-covalent interactions such as hydrogen bonding and ionic bonding, which play a critical role in their structure and function. Disulfide bonds are particularly important in stabilizing the tertiary structure of proteins, where sulfur atoms from cysteine residues oxidize to form a link. Ionic bonds occur between positively and negatively charged amino acid side chains, enhancing the molecule's stability. Hydrogen bonds, typically between oxygen or nitrogen atoms and hydrogen atoms, facilitate intramolecular and intermolecular interactions within peptides.