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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12F, a tight junction strand formed by the conserved hydrophobic residue that protrudes from the ECH in one protomer fits snugly into the hydrophobic pocket formed by TM3 and ECS2 in the adjacent protomer (Fig.
In this model, the longest [beta]-strand, [beta]-4, forms an antiparallel [beta]-sheet between the facing protomers and could be energetically favorable.
dagger]) Following the model of the hepatitis A virus protomer of Ming Luo (Figure 1).
Each sphere represents an actin monomer, which is strictly speaking a protomer of actin filaments, with the diameter of 5.
The actin protomer (monomer) appeared to be triangular in profile, with one end being convex and the other concave.
Toxin protomers must first bind to target membranes by either unidentified high-affinity receptors or through nonspecific absorption to substances such as phosphotidylcholine or cholesterol on the lipid bilayer (6-8).
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.
Human CRP consists of five identical protomers and each of these has a binding site for the many intrinsic and extrinsic ligands (9).
Crystal packaging and biochemical characteristics suggest that these proteins form hexameric units that may well represent protomers in the carboxysome assembly pathway.
When calcium-binding sites are not occupied, the protomers of CRP undergo structural changes and have a looser conformation (1, 13, 14), allowing for weaker interactions between the subunits.
We will determine whether picornavirus virions assemble from capsid protein protomers around the condensed genome or if the genome is packaged into a pre-formed empty capsid.
Human testosterone-binding globulin is a dimer composed of two identical protomers that are differently glycosylated.