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Once the oligomeric form is bound the interaction, as a result of avidity, becomes very strong.
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Laws bind the interactions of individual voices; no line is isolated; nothing is arbitrary.
Despite being non-covalently bound, the protein interactions made by the glucose molecule are identical to those observed for the covalently linked 2FGlc, the exception being that the acid/base catalyst Glu166 forms two hydrogen bonds to the Glc O1 hydroxyl group (Fig. 3e; Table S 2).
In somatic tissue the maternal DMR is unmethylated with CTCF bound, disrupting the interaction between the Rasgrf1 enhancer and promoter and subsequently inhibiting transcriptional activation.
The new antiprion compounds 3 and 6, which bind with the interaction energies of −12.1 and −13.2 kcal/mol, respectively, show fluorescence quenching with binding constant (Kd) values of 15.5 and 44.14 μM, respectively.
We will summarize the current research into mechanisms by which several diet factors bind to the interaction partners to transduce signals downstream and the implications for the disease-associated biology.
At time = 0 s the compound is injected on the protein surface and rapidly binds the immobilised protein, interaction is allowed to take place for 30 s, after which the injection stops and the compounds dissociate from the surface.
EspFu forms an amphipathic helix that binds the GBD, mimicking interactions of the VCA domain in autoinhibited WASP.
In other words, at early stages of heat shock or other stress stimulation increasing amounts of Mss4 protein efficiently bind the eIF3f preventing its interaction with CDK11p46.
The results suggest that MLE and MSL1 bind in close proximity to TopoII, but MSL2 and MSL3 bind beyond the interaction range.
Akt is phosphorylated at Y by the membrane bound Src via the interaction between its C-terminal proline-rich motif and the SH3 domain of Src.
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Since I tried Ludwig back in 2017, I have been constantly using it in both editing and translation. Ever since, I suggest it to my translators at ProSciEditing.

Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com