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An integral, or intrinsic, membrane protein (IMP) [1] is a type of membrane protein that is permanently attached to the biological membrane. All transmembrane proteins can be classified as IMPs, but not all IMPs are transmembrane proteins. [2] IMPs comprise a significant fraction of the proteins encoded in an organism's genome. [3]
Integral membrane proteins are a permanent part of a cell membrane and can either penetrate the membrane (transmembrane) or associate with one or the other side of a membrane (integral monotopic). Peripheral membrane proteins are transiently associated with the cell membrane.
Schematic representation of transmembrane proteins: 1) a single-pass membrane protein 2) a multipass membrane protein (α-helix) 3) a multipass membrane protein β-sheet. The membrane is represented in light yellow. A transmembrane protein is a type of integral membrane protein that spans the entirety of the cell membrane.
Cross-sectional view of the structures that can be formed by phospholipids in an aqueous solution. A biological membrane, biomembrane or cell membrane is a selectively permeable membrane that separates the interior of a cell from the external environment or creates intracellular compartments by serving as a boundary between one part of the cell and another.
Illustration of a eukaryotic cell membrane Comparison of a eukaryotic vs. a prokaryotic cell membrane. The cell membrane (also known as the plasma membrane or cytoplasmic membrane, and historically referred to as the plasmalemma) is a biological membrane that separates and protects the interior of a cell from the outside environment (the extracellular space).
Comparison of transport proteins. A symporter is an integral membrane protein that is involved in the transport of two (or more) different molecules across the cell membrane in the same direction. The symporter works in the plasma membrane and molecules are transported across the cell membrane at the same time, and is, therefore, a type of ...
The fluid property of functional biological membranes had been determined through labeling experiments, x-ray diffraction, and calorimetry.These studies showed that integral membrane proteins diffuse at rates affected by the viscosity of the lipid bilayer in which they were embedded, and demonstrated that the molecules within the cell membrane are dynamic rather than static.
The exception is the beta-4 subunit, which has a cytoplasmic domain of 1,088 amino acids, one of the largest of any membrane protein. Outside the cell membrane, the α and β chains lie close together along a length of about 23 nm; the final 5 nm N-termini of each chain forms a ligand-binding region for the ECM.