enow.com Web Search

Search results

  1. Results from the WOW.Com Content Network
  2. Integral membrane protein - Wikipedia

    en.wikipedia.org/wiki/Integral_membrane_protein

    Integral monotopic proteins are permanently attached to the cell membrane from one side. [5] Three-dimensional structures of the following integral monotopic proteins have been determined: [citation needed] prostaglandin H2 syntheses 1 and 2 (cyclooxygenases) lanosterol synthase and squalene-hopene cyclase; microsomal prostaglandin E synthase

  3. Hydrophobicity scales - Wikipedia

    en.wikipedia.org/wiki/Hydrophobicity_scales

    When consecutively measuring amino acids of a protein, changes in value indicate attraction of specific protein regions towards the hydrophobic region inside lipid bilayer. The hydrophobic or hydrophilic character of a compound or amino acid is its hydropathic character, [ 1 ] hydropathicity, or hydropathy.

  4. Membrane protein - Wikipedia

    en.wikipedia.org/wiki/Membrane_protein

    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. [citation needed]

  5. Membrane models - Wikipedia

    en.wikipedia.org/wiki/Membrane_models

    Integral proteins: Immersed in the bi-layer and held in place by the affinity of hydrophobic parts of the protein for the hydrophobic tails of phospholipids on interior of the layer. Peripheral proteins : More hydrophilic , and thus are non- covalently linked to the polar heads of phospholipids and other hydrophilic parts of other membrane ...

  6. Transmembrane protein - Wikipedia

    en.wikipedia.org/wiki/Transmembrane_protein

    The portion of the membrane proteins that are attached to the lipid bilayer (see annular lipid shell) consist mostly of hydrophobic amino acids. [13] Membrane proteins which have hydrophobic surfaces, are relatively flexible and are expressed at relatively low levels. This creates difficulties in obtaining enough protein and then growing crystals.

  7. Transmembrane domain - Wikipedia

    en.wikipedia.org/wiki/Transmembrane_domain

    A transmembrane domain (TMD, TM domain) is a membrane-spanning protein domain.TMDs may consist of one or several alpha-helices or a transmembrane beta barrel.Because the interior of the lipid bilayer is hydrophobic, the amino acid residues in TMDs are often hydrophobic, although proteins such as membrane pumps and ion channels can contain polar residues.

  8. Membrane transport - Wikipedia

    en.wikipedia.org/wiki/Membrane_transport

    This structure probably involves a conduit through hydrophilic protein environments that cause a disruption in the highly hydrophobic medium formed by the lipids. [1] These proteins can be involved in transport in a number of ways: they act as pumps driven by ATP, that is, by metabolic energy, or as channels of facilitated diffusion.

  9. Biological membrane - Wikipedia

    en.wikipedia.org/wiki/Biological_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.