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The spectrometer was calibrated by determining the binding energy values of Au 4f7/4 (84.0 eV), Ag 3d5/2 (368.4 eV), and Cu 2P3/2 (932.6 eV) levels using spectrograde materials.
The quantitative estimate of the stability of these solvates is established by determining the binding energy [1, 14, 16] for the solvents in all the solvates using equation 1 where the percent mass loss measured over the TG desolvation step of each solvate (ΔmS%) was related to the enthalpy change calculated over the corresponding DSC desolvation endotherm (ΔHSexp).
By determining the binding sites of individual FruM isoforms using SELEX we demonstrate that the distinct zinc finger domain of each FruM isoforms confers different DNA binding specificities.
By determining the binding profiles for Ler and Pch, we showed that both were involved in regulating one class of genes, but only Pch was involved in regulating the other class.
Biological activity and receptor binding properties were examined by measuring the IL-4 dose dependency of TF-1 cell proliferation as described (Tony et al., 1994) and by determining the binding affinity of the recombinant IL-4 protein to its high-affinity receptor IL-4Rα via surface plasmon resonance as published (Shen et al., 1996).
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Initial population frequencies of both BOXA and BOXC were obtained by determining the equilibrium binding site frequencies prior to the introduction of mutant SPC into the population.
Thus, we set out to identify the targets of Id inhibition by determining the direct binding partners of both Id and E proteins in ESCs.
Only uniquely mapped reads with a length of 36 bp were then used further for determining the binding regions by our BELT program [ 48].
We investigated this possibility by determining the specific ligand binding of I-PDGF-BB to PAE/NRP1 cells.
This study aimed to decipher the mechanics of p63 binding by determining the minimal in-vivo motif required for binding, distinguishing between chromatin architecture of bound and unbound motifs and identifying cooperating TFs that modulate p63 biological activity.
In addition, the potential binding of the polybasic domain of STIM1 to phosphoinositides may regulate the activity of the Orai1 channel by determining the extent of STIM1 Orai1 binding.
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