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Protein Regulation definitions

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  • Phosphorylation
    Reversible addition of phosphate groups, introducing negative charges that cause conformational changes and alter protein activity.
  • Glycosylation
    Reversible attachment of carbohydrates, such as oligosaccharides, to proteins, influencing their function and localization.
  • Ubiquitination
    Attachment of a small protein marker that targets proteins for degradation, controlling protein lifespan in the cell.
  • Cleavage
    Irreversible cutting of a protein segment, often altering its function, localization, or activation state.
  • GTP Binding
    Association of guanosine triphosphate with proteins, enabling activation or inactivation through conformational changes.
  • GTP Hydrolysis
    Conversion of GTP to GDP, typically resulting in protein inactivation and regulation of signaling pathways.
  • Calcium Binding
    Interaction with calcium ions, allowing proteins to respond to changes in cellular calcium concentration.
  • Protein Machine
    Complex of ten or more proteins with dynamic, interchangeable parts, requiring precise regulation for coordinated function.
  • Kinase
    Enzyme responsible for adding phosphate groups to proteins, modulating their activity.
  • Phosphatase
    Enzyme that removes phosphate groups from proteins, reversing phosphorylation effects.
  • O-Linked Glycosylation
    Attachment of carbohydrates to the oxygen atom of serine or threonine residues in proteins.
  • N-Linked Glycosylation
    Attachment of carbohydrates to the nitrogen atom of asparagine residues in proteins.
  • Lipid Modification
    Covalent addition of lipid groups to proteins, often anchoring them to membranes or altering their interactions.
  • Conformational Change
    Structural alteration in a protein, often triggered by modifications, that impacts its activity or interactions.
  • Degradation
    Process by which proteins are broken down, often following specific modifications that mark them for removal.