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Non-standard amino acids that are found in proteins are formed by post-translational modification, which is modification after translation during protein synthesis.
These modifications are often essential for the function or regulation of a protein ; for example, the carboxylation of glutamate allows for better binding of calcium cations, and the hydroxylation of proline is critical for maintaining connective tissues.
Another example is the formation of hypusine in the translation initiation factor EIF5A, through modification of a lysine residue.
Such modifications can also determine the localization of the protein, e. g., the addition of long hydrophobic groups can cause a protein to bind to a phospholipid membrane.

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