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The translation factor bound dimer has been suggested to have an increased affinity for the ribosome [54,61].
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These dimers have been isolated and characterized.
Various plasmonic dimers have been investigated, including nanosphere dimers [31], nanodisk dimers [32], and nanorod dimers [33].
The existence of loosely bound dimers of trimers has been reported for both endogenous and recombinant hPCNA after cross-linking with formaldehyde [15].
The apparent connection between DHPS catalysis and the dimer interface prompted us to look more closely at our previous YpDHPS crystal structures of the dimer in the apo conformation, the product-analogue-bound conformation, and the intermediate-state conformation in which DHPP and pABA had bound, PPi had been cleaved but not released, and the pterin-pABA bond had not been formed.
Another example is ddb2, which binds to damaged DNA that has been distorted by bulky lesions or cyclic pyrimidine dimers generated by exposure to UV light.
Although Thap1 has been proposed to dimerize and to bind DNA as a dimer [ 20, 21], there is insufficient data to conclude that it is a covalent bound dimer that would persist following our extraction procedures.
It retains two heparin binding sites and has been shown to bind heparin as a dimer [ 60].
It has been shown that Smad4 dimers can bind cooperatively to DNA even in the absence of direct physical contacts [ 30].
The tetrapeptide GPRP has been shown to bind to the D-dimer protein, a well known biomarker for thrombosis [ 39], with 25 μmol L−1 affinity [ 24].
A stronger signal of reporter protein expression has been demonstrated when either KorA or KorB dimers are bound alone.
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