Protein domain in the context of "Ion channels"

Lactase (EC 3.2.1.108) is an enzyme produced by many organisms and is essential to the complete digestion of whole milk. It breaks down the sugar lactose into its component parts, galactose and glucose, simple sugars that can be absorbed into the bloodstream through an animal's intestines. A lactase is a type of β-galactosidase because it breaks down the β-glycosidic bond in D-lactose. The chemical reaction it catalyzes is:

The only human gene encoding a lactase is LCT or lactase-phlorizin hydrolase (alternative symbol LPH). LCT has a lactase domain and a phlorizin hydrolase domain. It is encoded on chromosome 2. Lactase is found in the brush border of the small intestine of humans and other mammals. People deficient in LCT or lacking functional LCT may experience the symptoms of lactose intolerance after consuming milk products.

Ion channels are pore-forming membrane proteins that allow ions to pass through the channel pore. Their functions include establishing a resting membrane potential, shaping action potentials and other electrical signals by gating the flow of ions across the cell membrane, controlling the flow of ions across secretory and epithelial cells, and regulating cell volume. Ion channels are present in the membranes of all cells. Ion channels are one of the two classes of ionophoric proteins, the other being ion transporters.

The study of ion channels often involves biophysics, electrophysiology, and pharmacology, while using techniques including voltage clamp, patch clamp, immunohistochemistry, X-ray crystallography, fluoroscopy, and RT-PCR. Their classification as molecules is referred to as channelomics.

Chlamydomonas (/ˌklæmɪˈdɒmənəs, -dəˈmoʊ-/ KLAM-ih-DOM-ə-nəs, -⁠də-MOH-) is a genus of green algae consisting of about 150 species of unicellular flagellates, found in stagnant water and on damp soil, in freshwater, seawater, and even in snow as "snow algae". Chlamydomonas is used as a model organism for molecular biology, especially studies of flagellar motility and chloroplast dynamics, biogenesis, and genetics. One of the many striking features of Chlamydomonas is that it contains ion channels (channelrhodopsins) that are directly activated by light. Some regulatory systems of Chlamydomonas are more complex than their homologs in Gymnosperms, with evolutionarily related regulatory proteins being larger and containing additional domains.

Molecular phylogeny studies indicated that the traditional genus Chlamydomonas as defined using morphological data, was polyphyletic within Volvocales. Many species were subsequently reclassified (e.g., Oogamochlamys, Lobochlamys), and many other "Chlamydomonas" s.l. lineages are still to be reclassified.

Metalloprotein is a generic term for a protein that contains a metal ion cofactor. A large proportion of all proteins are part of this category. For instance, at least 1000 human proteins (out of ~20,000) contain zinc-binding protein domains although there may be up to 3000 human zinc metalloproteins.

A single-pass membrane protein also known as single-spanning protein or bitopic protein is a transmembrane protein that spans the lipid bilayer only once. These proteins may constitute up to 50% of all transmembrane proteins, depending on the organism, and contribute significantly to the network of interactions between different proteins in cells, including interactions via transmembrane alpha helices. They usually include one or several water-soluble protein domains situated at the different sides of biological membranes, for example in single-pass transmembrane receptors. Some of them are small and serve as regulatory or structure-stabilizing subunits in large multi-protein transmembrane complexes, such as photosystems or the respiratory chain. More than 2300 single-pass membrane proteins have been identified in the human genome.

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. TMDs vary greatly in size and hydrophobicity; they may adopt organelle-specific properties.

A DNA-binding domain (DBD) is an independently folded protein domain that contains at least one structural motif that recognizes double- or single-stranded DNA. A DBD can recognize a specific DNA sequence (a recognition sequence) or have a general affinity to DNA. Some DNA-binding domains may also include nucleic acids in their folded structure.

Protein tertiary structure is the three-dimensional shape of a protein. The tertiary structure will have a single polypeptide chain "backbone" with one or more protein secondary structures, the protein domains. Amino acid side chains and the backbone may interact and bond in a number of ways. The interactions and bonds of side chains within a particular protein determine its tertiary structure. The protein tertiary structure is defined by its atomic coordinates. These coordinates may refer either to a protein domain or to the entire tertiary structure. A number of these structures may bind to each other, forming a quaternary structure.