A membrane protein is a protein molecule that is attached to, or associated with the membrane of a cell or an organelle. More than half of all proteins interact with membranes.
Biological membranes consist of a phospholipid bilayer and a variety of proteins that accomplish vital biological functions. Structural proteins are attached to microfilaments in the cytoskeleton which ensures stability of the cell. Cell recognition proteins allow cells to identify each other and interact. Such proteins are involved in immune response, for example. Membrane enzymes produce a variety of substances essential for cell function. Membrane receptor proteins serve as connection between the cell's internal and external environments. Finally, transport proteins play an important role in the maintenance of concentrations of ions. These transport proteins come in two forms: carrier proteins and channel proteins. Carrier proteins are involved in using the energy released from ATP being broken down to facilitate active transport and ion exchange. These processes ensure that useful substances are able to enter the cell and that toxic substances are pumped out of the cell.
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Integral membrane proteins are permanently attached to the membrane. They can be defined as those proteins which require a detergent (such as SDS or Triton X-100) or some other apolar solvent to be displaced. They can be classified according to their relationship with the bilayer:
Peripheral membrane proteins are temporarily attached either to the lipid bilayer or to integral proteins by a combination of hydrophobic, electrostatic, and other non-covalent interactions. Peripheral proteins dissociate following treatment with a polar reagent, such as a solution with an elevated pH or high salt concentrations.
Integral and peripheral proteins may be post-translationally modified, with added fatty acid or prenyl chains, or GPI (glycosylphosphatidylinositol), which may be anchored in the lipid bilayer.
Classification of membrane proteins to integral and peripheral does not include some polypeptide toxins, such as colicin A or alpha-hemolysin, and certain proteins involved in apoptosis. These proteins are water-soluble but can aggregate and associate irreversibly with the lipid bilayer and form alpha-helical or beta-barrel transmembrane channels. An alternative classification is to divide all membrane proteins to integral and amphitropic.[1] The amphitropic are proteins that can exist in two alternative states: a water-soluble and a lipid bilayer-bound, whereas integral proteins can be found only in the membrane-bound state. The amphitropic protein category includes water-soluble channel-forming polypeptide toxins, which associate irreversibly with membranes, but excludes peripheral proteins that interact with other membrane proteins rather than with lipid bilayer.
Proteins are specifically targeted to many different types of biological membranes [2]
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