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A monomer (/ ˈ m ɒ n ə m ər / MON-ə-mər; mono-, "one" + -mer, "part") is a molecule that can react together with other monomer molecules to form a larger polymer chain or three-dimensional network in a process called polymerization.
The enzyme is a monomer, the isoenzymes are due to the differences in the carbohydrate content (sialic acid residues). The most important ALP isoenzymes are α 1-ALP, α 2-heat labile ALP, α 2-heat stable ALP, pre-β ALP and γ-ALP. Increase in α 2-heat labile ALP suggests hepatitis whereas pre-β ALP indicates bone diseases.
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.
The quaternary structure of this protein complex would be described as a homo-trimer because it is composed of three identical smaller protein subunits (also designated as monomers or protomers). The number of subunits in an oligomeric complex is described using names that end in -mer (Greek for "part, subunit"). Formal and Greco-Latinate names ...
Aquaporins form four-part clusters (tetramers) in the cell membrane, with each of the four monomers acting as a water channel. Different aquaporins have different sized water channels, the smallest types allowing nothing but water through. [29] X-ray profiles show that aquaporins have two conical entrances.
The uniformity of both specific types of molecules (the biomolecules) and of certain metabolic pathways are invariant features among the wide diversity of life forms; thus these biomolecules and metabolic pathways are referred to as "biochemical universals" [4] or "theory of material unity of the living beings", a unifying concept in biology ...
The lac repressor (LacI) operates by a helix-turn-helix motif in its DNA-binding domain, binding base-specifically to the major groove of the operator region of the lac operon, with base contacts also made by residues of symmetry-related alpha helices, the "hinge" helices, which bind deeply in the minor groove. [1]
For this reason, endopeptidases cannot break down peptides into monomers, while exopeptidases can break down proteins into monomers. A particular case of endopeptidase is the oligopeptidase, whose substrates are oligopeptides instead of proteins. They are usually very specific for certain amino acids. Examples of endopeptidases include: