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  2. Cell junction - Wikipedia

    en.wikipedia.org/wiki/Cell_junction

    Intermediate filaments composed of keratin or desmin are attached to membrane-associated attachment proteins that form a dense plaque on the cytoplasmic face of the membrane. Cadherin molecules form the actual anchor by attaching to the cytoplasmic plaque, extending through the membrane and binding strongly to cadherins coming through the ...

  3. Membrane protein - Wikipedia

    en.wikipedia.org/wiki/Membrane_protein

    In 2008, 150 unique structures of membrane proteins were available, [14] and by 2019 only 50 human membrane proteins had had their structures elucidated. [13] In contrast, approximately 25% of all proteins are membrane proteins. [15] Their hydrophobic surfaces make structural and especially functional characterization difficult.

  4. Tight junction - Wikipedia

    en.wikipedia.org/wiki/Tight_junction

    Depiction of the transmembrane proteins that make up tight junctions: occludin, claudins, and JAM proteins. Occludin was the first integral membrane protein to be identified. It has a molecular weight of ~60kDa. It consists of four transmembrane domains and both the N-terminus and the C-terminus of the protein are intracellular.

  5. Lipid-anchored protein - Wikipedia

    en.wikipedia.org/wiki/Lipid-anchored_protein

    The lipid-anchored protein can be located on either side of the cell membrane. Thus, the lipid serves to anchor the protein to the cell membrane. [1] [2] They are a type of proteolipids. The lipid groups play a role in protein interaction and can contribute to the function of the protein to which it is attached. [2]

  6. Cytosol - Wikipedia

    en.wikipedia.org/wiki/Cytosol

    This mixture of small molecules is extraordinarily complex, as the variety of molecules that are involved in metabolism (the metabolites) is immense. For example, up to 200,000 different small molecules might be made in plants, although not all these will be present in the same species, or in a single cell. [ 12 ]

  7. Ankyrin - Wikipedia

    en.wikipedia.org/wiki/Ankyrin

    The interactions the sites use to bind to membrane proteins are non-specific and consist of: hydrogen bonding, hydrophobic interactions and electrostatic interactions. These non-specific interactions give ankyrin the property to recognise a large range of proteins as the sequence doesn't have to be conserved, just the properties of the amino ...

  8. Transmembrane protein - Wikipedia

    en.wikipedia.org/wiki/Transmembrane_protein

    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.

  9. Peripheral membrane protein - Wikipedia

    en.wikipedia.org/wiki/Peripheral_membrane_protein

    The regulatory protein subunits of many ion channels and transmembrane receptors, for example, may be defined as peripheral membrane proteins. In contrast to integral membrane proteins, peripheral membrane proteins tend to collect in the water-soluble component, or fraction, of all the proteins extracted during a protein purification procedure.