Final answer:
Amino acids can undergo post-translational modifications such as phosphorylation or glycosylation, which are important for protein functionality and diversification. Modifications can also result in the formation of amino acid derivatives, impacting cellular processes and drug design strategies.
Step-by-step explanation:
Amino acids can become modified through various post-translational modifications (PTMs) once a protein has been synthesized. Examples of such modifications include the enzymatic removal of the N-formyl methionine in prokaryotes or methionine in eukaryotes at the start of the protein sequence, and sometimes, acetylation of the N-terminal amino acid residue. Additionally, modifications like phosphorylation or glycosylation may occur, where phosphate groups or sugar molecules are added to specific amino acids in the protein chain, significantly diversifying and enhancing protein function.
In some instances, amino acids in proteins are derivatives of the common 20 amino acids, such as hydroxyproline derived from proline. These modifications can alter the properties and activities of proteins, which are crucial in cellular processes. The synthesis of amino acid prodrugs in pharmaceuticals also relies on the stable properties of modified amino acids, both naturally occurring and synthetic. Therefore, the modification of amino acids is a vital aspect of protein function and drug development.