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  2. Biological membrane - Wikipedia

    en.wikipedia.org/wiki/Biological_membrane

    Biological molecules are amphiphilic or amphipathic, i.e. are simultaneously hydrophobic and hydrophilic. [6] The phospholipid bilayer contains charged hydrophilic headgroups, which interact with polar water. The layers also contain hydrophobic tails, which meet with the hydrophobic

  3. 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.

  4. Hydrophobe - Wikipedia

    en.wikipedia.org/wiki/Hydrophobe

    Water on hydrophobic surfaces will exhibit a high contact angle. Examples of hydrophobic molecules include the alkanes, oils, fats, and greasy substances in general. Hydrophobic materials are used for oil removal from water, the management of oil spills, and chemical separation processes to remove non-polar substances from polar compounds. [2]

  5. 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.

  6. Integral membrane protein - Wikipedia

    en.wikipedia.org/wiki/Integral_membrane_protein

    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]

  7. 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.

  8. Glycerophospholipid - Wikipedia

    en.wikipedia.org/wiki/Glycerophospholipid

    Each glycerophospholipid molecule consists of a small polar head group and two long hydrophobic chains. In the cell membrane, the two layers of phospholipids are arranged as follows: the hydrophobic tails point to each other and form a fatty, hydrophobic center; the ionic head groups are placed at the inner and outer surfaces of the cell membrane

  9. Hydrophobic effect - Wikipedia

    en.wikipedia.org/wiki/Hydrophobic_effect

    [1] [2] The word hydrophobic literally means "water-fearing", and it describes the segregation of water and nonpolar substances, which maximizes the entropy of water and minimizes the area of contact between water and nonpolar molecules. In terms of thermodynamics, the hydrophobic effect is the free energy change of water surrounding a solute. [3]