Protein quaternary structureProtein quaternary structure is the fourth (and highest) classification level of protein structure. Protein quaternary structure refers to the structure of proteins which are themselves composed of two or more smaller protein chains (also referred to as subunits). Protein quaternary structure describes the number and arrangement of multiple folded protein subunits in a multi-subunit complex.
DimerizationIn chemistry, dimerization is the process of joining two identical or similar molecular entities by bonds. The resulting bonds can be either strong or weak. Many symmetrical chemical species are described as dimers, even when the monomer is unknown or highly unstable. The term homodimer is used when the two subunits are identical (e.g. A–A) and heterodimer when they are not (e.g. A–B). The reverse of dimerization is often called dissociation.
ProteinBiomolecule consisting of chains of amino acid residuesA representation of the 3D structure of the protein myoglobin showing turquoise α-helices. This protein was the first to have its structure solved by X-ray crystallography. Toward the right-center among the coils, a prosthetic group called a heme group (shown in gray) with a bound oxygen molecule (red).Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acidresidues.BiochemistryStudy of chemical processes of living organismsBiochemistry, or biological chemistry (distinct from chemical biology), is the study of chemical processes within and relating to living organisms. A sub-discipline of both chemistry and biology, biochemistry may be divided into three fields: structural biology, enzymology, and metabolism. Over the last decades of the 20th century, biochemistry has become successful at explaining living processes through these three disciplines.
MonomerA monomer ( ; , "one" + , "part") is a molecule that can react together with other monomer molecules to form a larger polymer chain or two- or three-dimensional network in a process called polymerization.IUPAC definitionMonomer molecule: A molecule which can undergo polymerization, thereby contributing constitutional units to the essential structure of a macromolecule.
IKBKGMore reference expression dataBioGPSEnsemblUniProtRefSeq (mRNA)RefSeq (protein)Location (UCSC)Chr X: 154.54 – 154.57 MbChr X: 73.44 – 73.5 MbPubMed searchWikidataNF-kappa-B essential modulator (NEMO) also known as inhibitor of nuclear factor kappa-B kinase subunit gamma (IKK-γ) is a protein that in humans is encoded by the IKBKGgene. NEMO is a subunit of the IκB kinase complex that activates NF-κB. The human gene for IKBKG is located on the chromosome band Xq28.
Amino acidOrganic compounds containing amine and carboxylic groupsStructure of a typical L-alpha-amino acid in the "neutral" formAmino acids are organic compounds that contain both amino and carboxylic acidfunctional groups. Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. Only these 22 appear in the genetic code of life.
Reverse transcriptaseA reverse transcriptase (RT) is an enzyme that uses an RNA molecule as a template to synthesize a complementary DNA molecule, through a process termed reverse transcription. Reverse transcriptases are used by viruses such as HIV and hepatitis B to replicate their genomes, by retrotransposon mobile genetic elements to proliferate within the host genome, and by eukaryotic cells to extend the telomeres at the ends of their linear chromosomes.
Nucleic acidNucleic acids are large biomolecules that are crucial in all cells and viruses. They are composed of nucleotides, which are the monomer components: a 5-carbon sugar, a phosphate group and a nitrogenous base. The two main classes of nucleic acids are deoxyribonucleic acid (DNA) and ribonucleic acid (RNA). If the sugar is ribose, the polymer is RNA; if the sugar is deoxyribose, a variant of ribose, the polymer is DNA.
Non-covalent interactionIn chemistry, a non-covalent interaction differs from a covalent bond in that it does not involve the sharing of electrons, but rather involves more dispersed variations of electromagnetic interactions between molecules or within a molecule. The chemical energy released in the formation of non-covalent interactions is typically on the order of 1–5 kcal/mol (1000–5000 calories per 6.02×10 molecules).
Covalent bondA covalent bond is a chemical bond that involves the sharing of electrons to form electron pairs between atoms. These electron pairs are known as shared pairs or bonding pairs. The stable balance of attractive and repulsive forces between atoms, when they share electrons, is known as covalent bonding. For many molecules, the sharing of electrons allows each atom to attain the equivalent of a full valence shell, corresponding to a stable electronic configuration.DisulfideIn chemistry, a disulfide (or disulphide in British English) is a compound containing a R−S−S−R′ functional group or the S22− anion. In inorganic chemistry, the anion appears in the common mineral pyrite but is otherwise rare. Compounds of the form R−S−S−H are usually called persulfides instead. Disulfide bridges also appear as a common post-translational modification in proteins.*As an Amazon Associate I earn from qualifying purchases.