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To characterize the receptor binding properties of wild type and mutated FIV PPR SUs, we used a series of continuous and engineered cell lines (Figure 1).
A non-radioactive electrophoretic mobility shift assay (EMSA) method was used to inspect the DNA binding properties of wild type and mutant TTE-M2S1 complexes.
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The dynamics and ligand binding properties of wild-type and mutant LckSH3 were studied by fluorescence and NMR spectroscopy as well as molecular dynamics simulations.
Here, we report primarily on the impact of N-terminal acetylation on the structural and lipid binding properties of wild-type aS (lacking the His tag), as viewed by NMR and CD spectroscopy.
Nevertheless, the different Bim1 binding properties of wild-type and mutant microtubules provide strong support for the idea that the mutant retains significant GTP-lattice-like character in a GDP lattice.
Finally, the ligand-binding properties of wild-type and variant 2G12-IgMs were assessed by ELISA and neutralization assays.
In conclusion, in the present study we have systematically analysed the lipid-binding properties of wild-type JP2 and the S101R mutant with the findings offering new insights into the role of this protein in dyad organization and how changes to the structural characteristics of the JP2 may play a role in the pathogenesis of disease.
Since both PAR-1 and Shaggy seem to play an important role in affecting the physiological properties of tau, our next step was to test the effects of the individual kinases on the microtubule-binding properties of wild-type and S2A tau.
To assess whether the resistance properties of spores containing Ssp4 with a site-directed mutation at residue 36 correlated with the DNA binding properties of their Ssp4 variant, wild-type SM101 rSsp4, the SM101 rsite-directedected mutants, and wild-type F4969 rSsp4 were each purified and tested (Fig. 1C) for their DNA binding properties using an EMSA assay.
We designed in vitro assays to ask whether such alterations might reflect changes in chromatin, DNA and/or histone binding properties of progerin compared to wild-type lamin C-terminal tails.
However, the variant did not differ from the wild-type with respect to the binding properties of the antagonists (R -3- 2- 2- 4-methylpiperidin-1-yl)ethyl)-pyR -3- 2- 2- 4-methylpiperidin-1-ylhloR -3- 2- 2- 4-methylpiperidin-1-yluleR -3- 2- 2- 4-methylpiperidin-1-yl
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