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  2. Integral membrane protein - Wikipedia

    en.wikipedia.org/wiki/Integral_membrane_protein

    Since integral proteins span the width of the phospholipid bilayer, their extraction involves disrupting the phospholipids surrounding them, without causing any damage that would interrupt the function or structure of the proteins. Several successful methods are available for performing the extraction including the uses of "detergents, low ...

  3. Membrane protein - Wikipedia

    en.wikipedia.org/wiki/Membrane_protein

    Integral polytopic proteins are transmembrane proteins that span across the membrane more than once. These proteins may have different transmembrane topology. [4] [5] These proteins have one of two structural architectures: Helix bundle proteins, which are present in all types of biological membranes;

  4. Biological membrane - Wikipedia

    en.wikipedia.org/wiki/Biological_membrane

    Phospholipid bilayers contain different proteins. These membrane proteins have various functions and characteristics and catalyze different chemical reactions. Integral proteins span the membranes with different domains on either side. [6] Integral proteins hold strong association with the lipid bilayer and cannot easily become detached. [9]

  5. Cell membrane - Wikipedia

    en.wikipedia.org/wiki/Cell_membrane

    The protein itself is not in contact with the membrane. G proteins: Peripheral proteins: Attached to integral membrane proteins, or associated with peripheral regions of the lipid bilayer. These proteins tend to have only temporary interactions with biological membranes, and once reacted, the molecule dissociates to carry on its work in the ...

  6. Transmembrane protein - Wikipedia

    en.wikipedia.org/wiki/Transmembrane_protein

    Alpha-helical proteins are present in the inner membranes of bacterial cells or the plasma membrane of eukaryotic cells, and sometimes in the bacterial outer membrane. [5] This is the major category of transmembrane proteins. In humans, 27% of all proteins have been estimated to be alpha-helical membrane proteins. [6]

  7. Aquaporin - Wikipedia

    en.wikipedia.org/wiki/Aquaporin

    Schematic diagram of the 2D structure of aquaporin 1 depicting the six transmembrane alpha-helices and the five interhelical loop regions A-E The 3D structure of aquaporin Z highlighting the 'hourglass'-shaped water channel that cuts through the center of the protein. Aquaporin proteins are composed of a bundle of six transmembrane α-helices ...

  8. Cell adhesion molecule - Wikipedia

    en.wikipedia.org/wiki/Cell_adhesion_molecule

    In fully developed animals, these molecules play an integral role in generating force and movement and consequently ensuring that organs are able to execute their functions normally. [3] In addition to serving as "molecular glue", CAMs play important roles in the cellular mechanisms of growth, contact inhibition, and apoptosis.

  9. Intramembrane protease - Wikipedia

    en.wikipedia.org/wiki/Intramembrane_protease

    Intramembrane proteases are integral membrane proteins that are polytopic transmembrane proteins with multiple transmembrane helices. [5] [17] Their active sites are located within the transmembrane helices and form an aqueous environment within the hydrophobic lipid bilayer.