Post-translational regulation occurs within a cell when the newly formed protein is modified.
After being synthesized, folded, and put together, proteins can undergo post-translational modification. It has been shown that a variety of post-translational changes take place inside cells. Any alteration that can be made to a protein can also be undone. A post-translational alteration can take many distinct forms.
The process generally entails the formation of a covalent bond connecting a particular chemical group to a particular set of amino acid side chains on the protein. These groups can include phosphate groups (phosphorylation), acetate groups (acetylation), the attachment of lipid/hydrophobic groups (lipid modification), or carbohydrates (glycosylation). The majority of these post-translational changes are reversible; one enzyme adds the modifying group, and another enzyme can take it away.
For example, protein kinases phosphorylate proteins, while protein phosphatases remove such phosphate groups. Similar to allosteric effectors, post-translational changes alter the structure of the polypeptide to which they are bound, which therefore affects the polypeptide's activity. Additionally, they can alter a protein's stability, localization within the cell, and interactions with other proteins.
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