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  2. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    In biology and biochemistry, the active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction. The active site consists of amino acid residues that form temporary bonds with the substrate, the binding site, and residues that catalyse a reaction of that substrate, the catalytic site.

  3. Molecular binding - Wikipedia

    en.wikipedia.org/wiki/Molecular_binding

    Among the tightest known protein–protein complexes is that between the enzyme angiogenin and ribonuclease inhibitor; the dissociation constant for the human proteins is 5x10 −16 mol/L. [3] [4] Another biological example is the binding protein streptavidin, which has extraordinarily high affinity for biotin (vitamin B7/H, dissociation ...

  4. Protein domain - Wikipedia

    en.wikipedia.org/wiki/Protein_domain

    An example of a superdomain is the protein tyrosine phosphatase–C2 domain pair in PTEN, tensin, auxilin and the membrane protein TPTE2. This superdomain is found in proteins in animals, plants and fungi. A key feature of the PTP-C2 superdomain is amino acid residue conservation in the domain interface.

  5. Protein - Wikipedia

    en.wikipedia.org/wiki/Protein

    Each protein has its own unique amino acid sequence that is specified by the nucleotide sequence of the gene encoding this protein. The genetic code is a set of three-nucleotide sets called codons and each three-nucleotide combination designates an amino acid, for example AUG (adenine–uracil–guanine) is the code for methionine.

  6. Binding site - Wikipedia

    en.wikipedia.org/wiki/Binding_site

    Binding site in blue, inhibitor in green, and substrate in black. In the scope of cancer, ligands that are edited to have a similar appearance to the natural ligand are used to inhibit tumor growth. For example, Methotrexate, a chemotherapeutic, acts as a competitive inhibitor at the dihydrofolate reductase active site. [40]

  7. Alpha helix - Wikipedia

    en.wikipedia.org/wiki/Alpha_helix

    The alpha helix is also commonly called a: Pauling–Corey–Branson α-helix (from the names of three scientists who described its structure); 3.6 13-helix because there are 3.6 amino acids in one ring, with 13 atoms being involved in the ring formed by the hydrogen bond (starting with amidic hydrogen and ending with carbonyl oxygen)

  8. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    The existing specialized amino acid sequence compressors are low compared with that of DNA sequence compressors, mainly because of the characteristics of the data. For example, modeling inversions is harder because of the reverse information loss (from amino acids to DNA sequence).

  9. RING finger domain - Wikipedia

    en.wikipedia.org/wiki/RING_finger_domain

    In molecular biology, a RING (short for Really Interesting New Gene) finger domain is a protein structural domain of zinc finger type which contains a C 3 HC 4 amino acid motif which binds two zinc cations (seven cysteines and one histidine arranged non-consecutively).