Examples of using Dimer in English and their translations into Russian
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RNA: consists of a dimer RNA.
A protein dimer is a type of protein quaternary structure.
Cyclopentadiene, 1,2,3,4,5,5-hexachloro-, dimer;
Dimer- a turn near the gate of the former presidential residence.
To function, CD8 forms a dimer, consisting of a pair of CD8 chains.
The dimer model counts the number of dimer coverings of a graph.
Chemiluminescence occurs when singlet oxygen dimer decomposes.
An SMC2-SMC4 dimer has an ability to reanneal complementary single-stranded DNA.
A relatively large shift forms nanoclusters of«bucket»and«dimer» type.
In 1997 spectroscopic analysis revealed the dimer(or diatomic) absorption features of molecular oxygen.
Daxx serves as an H3.3 specific histone chaperone, interacting with an H3.3/H4 dimer.
This dimer assembles(more loosely) with another of its kind to form the four subunit complex.
PMT records chemiluminescence of the process of singlet oxygen dimer formation and decomposition.
Complex V can be found co-migrating as a dimer with other supercomplexes, but scarcely as part of the supercomplex unit.
PFK1 is an allosteric enzyme and has a structure similar to that of hemoglobin in so far as it is a dimer of a dimer. .
The process starts when light is absorbed by two BChl molecules(a dimer) that lie near the periplasmic side of the membrane.
MutS forms a dimer(MutS2) that recognises the mismatched base on the daughter strand and binds the mutated DNA.
At room temperature, pairs of these radicals join via their cyclopentadienyl rings to form a dimer, a yellow solid.
Electronic structure of Cerium(Ce 2) dimer and its influence on the phase transitions in the crystallic state of Cerium are studied.
Finally, the N-terminal region modulates PFK-2 and FBPase2 activities,and stabilizes the dimer form of the enzyme.
Two of these dimer structures then join side by side, in an antiparallel arrangement, to form a tetramer called a protofilament.
As has been stated in the present study and was shown in the work[8],chemiluminescence in Fenton's reaction is due to singlet oxygen dimer decomposition.
Each MetJ dimer contains two binding sites for the cofactor S-Adenosyl methionine(SAM) which is a product in the biosynthesis of methionine.
X-ray crystallography has shown two molecules of human surviving coming together to form a bowtie-shape dimer through a hydrophobic interface.
The first excimer laser used a xenon dimer(Xe2) energized by a beam of electrons to produce stimulated emission at an ultraviolet wavelength of 176 nm.
In another study[13]the authors used luminol to intensify light output, though the sensitivity of modern luminometers is enough to record singlet oxygen dimer alone.
Once bound, the MetJ dimer interacts with another MetJ dimer bound to the complementary strand of the operator via its alpha helices.
The enzyme acts by electron transfer in which the reduced flavin FADH-is activated by light energy and acts as an electron donor to break the pyrimidine dimer.
D-dimer(or D dimer) is a fibrin degradation product(or FDP), a small protein fragment present in the blood after a blood clot is degraded by fibrinolysis.
For EGFR gene, ErbB-2 acts as a coreceptor at the moment of forming dimer complex and later autophosphorylation, but the ligand has not been defined as yet 4.