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Binding started to plateau around 100nM and half-maximal binding was achieved at ≈3nM of DARPin 57.2.
The half-maximal binding was achieved at 2.4±0.4 nM and 43±4 nM of the purified β2GPI in the presence and in the absence of anti-β2GPI antibodies, respectively (Figure 4A).
Half-maximal binding was achieved at a fibrinogen concentration of ~70 nM.
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In other words, a stronger 'power-stroke' associated with ATP binding is achieved at the expense of reducing the hydrolysis power of the bound ATP.
For the two compounds, full saturation (corresponding to spectral invariance with increasing DNA concentration) is attained at [DNA]/[compound] = 200, meaning that total binding is achieved at this ratio.
Complete binding were achieved at ~0.5, ~1.0, ~1.0, and ~3.0 carrier:DNA ratios for branched PEI, PLL, PLL-PA, and Lipofectamine-2000™ Lipofectamine-2000™
The Fe-H bonds were formed, and their bindings were achieved at the expense of their Fe-Fe, Fe-Ni, and Ni-Ni first neighbors.
The maximum percentage of binding was obtained at a protein:nanoparticle weight ratio of 1 1, at which 94% binding was achieved.
DNA binding activity of NFκB induced by Cr VI) reached to peak at 3 hr, whereas the maximum AP-1 DNA binding activity was achieved at 9 hr after exposure.
Importantly, saturating levels of gp41 MPER binding was attained at 10 µg/106 splenocytes, when ∼25% of all B cells were labeled, the highest gp41 MPER/scrambled gp41 MPER binding ratio was achieved at the sub-saturating concentration of 100 ng/106 splenocytes.
Significant binding and uptake was achieved at aE-selectin densities as low as 400 molecules/μm2.
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