protomer


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pro·to·mer

(prō'tō-mĕr),
A structural subunit of a larger structure. Protomers may themselves consist of subunits. For example, tubulin, an αβ dimer, is the protomer for microtubules.
[G. protos, first, + -mer 1]
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This of course does not mean independently of any theory: for example, protomers are identifiable within the theory of chemical structure of molecules which involves many highly theoretical principles, but although it is T'-theoretical (for some other theory T'), the notion of protomer is not MWC-theoretical.
ToCDS formed an obligate functional dimer, with 3882 [[Angstrom].sup.2] buried at the dimer interface out of 16,979 [[Angstrom].sup.2] of each protomer's solvent accessible surface.
In the crystal lattice, the claudin protomers form a linear polymer structure.
LLO engages cholesterol as a native membrane receptor in dependence on the two amino acids threonine 515 and leucine 516, oligomerises to a prepore complex of up to 50 monomers, and forms a membrane pore in a concerted refolding step with each protomer contributing two betahairpins to the membrane-spanning [beta]-barrel, which originates from five a-helices in the soluble state [16, 59-61].
In the absence of avidin in the assay mixture, the activity of acetyl-CoA carboxylase is a measure of both the active polymeric and the activated protomeric since the inactive protomers are able to polymerise into the active form in the presence of citrate in the assay mixture.
Each sphere represents an actin monomer, which is strictly speaking a protomer of actin filaments, with the diameter of 5.5 nm.
The replaced amino acids were located in a refined 3-dimensional computer model of the HAV protomer (11), and their relative distances to residues 1102, 1171 and 1176, constituents of the immunodominant site (12), and to residue 1221, constituent of the glycophorin A binding site epitope (13), were used as markers of the potential antibody-escaping phenotype.
The functional CRP protomer is composed of two molecules of CRP, each being associated with cAMP.
The structure of CRP contains a crystal contact where the calcium-binding loop from one protomer coordinates into the calcium site of a second protomer to form the pentameric structure (Fig.
The secreted mature toxin, or protomer, is a hydrophilic molecule that lacks cysteine residues and has a molecular mass of approximately 33 kDa (6-8).
Two of the 3 protomers are displayed with high transparency to aid visualization.