Membrane Proteins
- Integral proteins are membrane proteins held within the lipid bilayer by hydrophobic interactions.
- Hydrophobic interactions allow nonpolar regions of integral proteins to associate with the fatty interior of the membrane.
- Transmembrane proteins are integral proteins that span the membrane from one side to the other.
- Ion channels, transport proteins, receptors, and guanosine triphosphate-binding proteins are important examples of integral membrane proteins.
- Guanosine triphosphate-binding proteins (G proteins) help transfer signals from activated receptors to intracellular signaling pathways.
- Peripheral proteins attach to the membrane surface without being embedded in the lipid bilayer.
- Electrostatic interactions are attractions between charged regions, and peripheral proteins can use these weak attractions to attach loosely to membranes.
- A covalent bond is a strong chemical bond in which atoms share electrons, so a protein that is not covalently attached can detach more easily than a protein joined by this stronger bond.
- Peripheral proteins are not covalently attached to membrane components, so their membrane association is usually less permanent than that of integral proteins.
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