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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.
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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.
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.
Sequence-specific binding is achieved by in situ hybridization of the primary probes to the genomic DNA.
The activity of MZ1 is dependent on binding to VHL but is achieved at a sufficiently low concentration not to induce stabilization of HIF-1α.
The maximum percentage of binding was obtained at a protein:nanoparticle weight ratio of 1 1, at which 94% binding was achieved.
Significance is achieved at P<0.05.
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