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The nucleophilic water molecule is displaced and a unique mode of binding is observed with the S-OH of the inhibitor occupying the oxyanion binding site of the proposed tetrahedral intermediate.
If a similar oligonucleotide junction is used that does not contain ICRIII (Junction 2 in Figure 2), much weaker binding is observed with a Kapp of 379 nM (inset Figure 3a).
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The GST-p53(295–390) mutant keeps the ability to bind PATZ1, whereas no binding was observed with the GST-p53(13–295).
Using GST or GST-NEMO as bait proteins (Figure 3A), we found that each of the five interactors was able to specifically bind GST-NEMO, while little or no binding was observed with the GST control (Figure 3B).
Evidence of disulfide bond formation was observed with the [B20H17SH]4− anion, whereas no evidence of covalent binding was observed with the [B20H18]2− and [B20H17OH]4− ions.
Highest cooperative binding was observed with DNA having maximum T-T mispairs which was supplemented by detailed UV-visible thermal analysis of DNA-Hg II) structures.
It bound specifically to the constant region of the rabbit IgG, and no binding was observed with mouse or goat IgG.
No binding was observed with biotinylated-BSA alone (Fig 1C), indicating specific binding to the INr peptides.
By contrast to these fragments, no binding was observed with htt fragments of amino acid 1-230, or smaller.
Similar specific binding was observed with the opposite combination, i.e., plate-bound CD58-BV and CD2-BV in solution (Fig. 2C).
By contrast, no significant inhibition of CD4 binding was observed with the GST-Arf1 (right panel) and GST (not shown) controls at the concentration of 120 µg/ml.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com