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Post Translational Modification definitions

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  • Post-translational Modification
    Covalent alteration made to a protein after translation, crucial for controlling protein activity and function.
  • Methylation
    Addition of a methyl group to a protein, often influencing its activity or interactions with other molecules.
  • Acetylation
    Attachment of an acetyl group to a protein, which can affect protein stability and regulatory functions.
  • Ubiquitination
    Covalent addition of a small protein called ubiquitin, marking proteins for degradation or altering their cellular location.
  • Phosphorylation
    Addition of a phosphate group to a protein, commonly used to regulate enzyme activity and signal transduction.
  • Hydroxylation
    Incorporation of a hydroxyl group into a protein, often modifying its structural properties or stability.
  • Lipidation
    Attachment of a lipid molecule to a protein, facilitating membrane association or signaling roles.
  • Disulfide Bond
    Covalent linkage between two cysteine residues, stabilizing protein structure or connecting polypeptide chains.
  • Sulfonation
    Addition of a sulfate group to a protein, which can influence protein interactions and function.
  • Glycosylation
    Attachment of a carbohydrate group to a protein, affecting folding, stability, and cell recognition.
  • Proteolytic Cleavage
    Breakage of peptide bonds within a protein by proteases or peptidases, often activating or deactivating the protein.
  • Protease
    Enzyme responsible for cleaving peptide bonds in proteins, enabling activation or processing of protein molecules.
  • Peptidase
    Enzyme that specifically targets peptide bonds, facilitating protein maturation or degradation.
  • Zymogen
    Inactive precursor form of a protein that requires proteolytic cleavage for activation.