pentamer

(redirected from pentameric)

vi·ri·on

(vī'rē-on, vir'ē-on),
The complete virus particle that is structurally intact and infectious.

pentamer

a polymer formed from five molecules of a monomer.
References in periodicals archive ?
Besides C-C coupled oligomeric structures we also found highintensity mass spectra peaks corresponding to tetrameric, pentameric, and hexameric molecules, which formed in the C-O coupling reaction or even two or three C-O coupling reactions.
zeylanicum bark with pentameric type-A procyanidine flavonoid as a marker compound (75.
A] receptors are pentameric ligand-gated chloride ion channels that are activated by binding gamma-aminobutyric acid (GABA), the main inhibitory neurotransmitter in the central nervous system (Sieghart 2006).
CRP is a 224-residue protein with an annular, pentameric disc shape.
IgM is the most primitive and least specialized immunoglobulin with a pentameric structure.
Oligomerization of Vibrio cholerae cytolysin yields a pentameric pore and has a dual specificity for cholesterol and sphingolipids in the target membrane.
Like the nicotinic cholinoceptor, it is a pentameric structure and modern techniques of genetic engineering (in particular the production of "knock-out" and "knock-in" mice) have been employed to determine the influences of those five protein strands on the properties of the receptors.
The highly variable pentameric repeats of the AT-rich germline limited DNA in Parascaris univalens are the telomeric repeats of somatic chromosomes.
4 Chocolate, or more specifically, the pentameric procyandin chemical found in cocoa, knocks out some of the proteins which can produce cancer.
It is a pentameric complex that contains four subunits a, b, g, and d in molar ratio 2:1:1:1.
The GABAA receptor is a chloride-conducting receptor composed most frequently of alpha, beta, and gamma subunits assembled as a pentameric structure, forming a central pore; but other subunit compositions are also possible (Sieghart 1995; Olsen and Sieghart 2008).
CRP is a pentameric protein composed of 5 identical subunits noncovalently bound together in radial symmetry around a central pore (1).