homodimer


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Related to homodimer: Heterodimer

homodimer

(hō-mō-dī'mĕr),
A molecule composed of paired identical proteins.
[homo- + dimer]

homodimer

a protein composed of two identical polypeptide chains.
References in periodicals archive ?
In Figure 8 (a) ethidium homodimer reacts with cells scaffold QS/FGS and upon binding red acid fluorescence can be observed, where gray cells are displayed on a dark background and of a rounded shape, because they did not extend to adhere to the nanofibers, indicating cell death.
Analysis of HER2 status by HERmark in approximately 900 patient samples from the FINHER study of Herceptin in the adjuvant setting to assess the relationship of HER2 protein and HER2:HER2 homodimer measurements with clinical outcomes.
Thymidylate synthase (TS) is a homodimer of approximately 72 kDa which catalyzes the reductive methylation of 2-deoxyuridine monophosphate (dUMP) using 5,10-methylenetetrahydrofolate ([CH.
The X-ray crystal structure shows that the enzyme exists as a homodimer, consisting of 30 kDa subunits.
and will evaluate the safety and therapeutic potential of escalating doses of a one-time injection of pure recombinant human platelet-derived growth factor (rhPDGF-BB) homodimer solution into the extensor carpi radialis brevis (ECRB), the tendon in the elbow that is generally the source of pain in tennis elbow.
Since no interaction could be formed between R43 and V31, the formation of NLRP3 homodimer has been largely compromised by this p.
It should be mentgioned, that SOD1, or Cu,Zn-SOD, was the first enzyme of this family to be characterised and is a copper and zinc-containing homodimer that is found almost exclusively in intracellular cytoplasmic spaces.
Upon JH binding to the PAS-B domain, Met undergoes a conformational change that liberates Met from the homodimer complex and allows it to bind Taiman [43,45-47].
Homocysteine is detected in amino acid profiles as its oxidized homodimer, homocystine.
Additionally biochemical studies suggest that transitory interaction between two N-terminal domains of the HSP90 homodimer occurs in an ATP dependent manner, and this provides the mechanistic basis for the ATPase driven molecular clamp.
From the chemical point of view AMH is a peptide homodimer of molecular weight 140 kDa, consisting of two identical glycoprotein subunits, connected by disulfide bridges.
Thyroid hormone receptor monomer, homodimer, and heterodimer (with retinoid-X receptor) contact different nucleotide sequences in thyroid hormone response elements.