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A series of biophysical experiments were performed to ascertain the binding mode between ticlopidine and calf thymus DNA.
Molecular modeling studies were carried out to ascertain the binding of the model compound to the active site of β-tubulin.
Therefore, to confirm such a hypothesis requires significant future work such as building a Nav1.8 homology model and conducting molecular dynamics simulations to ascertain the binding affinity of the [Lys]-fullerene.
To further ascertain the binding results and to determine whether these results are functionally significant we conducted killing assays using peripheral NK clones which express one of the NK inhibitory receptors, LIR-1 (Fig. 4A), KIR2DL1 (Fig. 4B) and KIR2DL2 (Fig. 4C).
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In silico molecular modeling methods, such as docking can aid in the drug discovery process by ascertaining the binding affinities of existing and hypothetical compounds towards PfTrxR and the human isoform of this enzyme.
Several other spectroscopic experiments such as circular dichromism (CD), iodide induced quenching, competitive binding assay with known groove binder probe, 3-hydroxyflavone (3HF), time resolved fluorescence decay measurements, thermometric experiment in connection with the helix melting of ctDNA etc. unequivocally ascertain the groove binding interaction of DSDP with ctDNA.
In the present study, we have attempted to ascertain the mode of binding of coumarin with calf thymus DNA (Ct-DNA) through various biophysical techniques.
Interaction of 1 and 3 with CT DNA was carried out by optical methods to ascertain the mode of binding, mechanism of action and their therapeutic potential.
To further ascertain the specificity of binding, we demonstrated that the formation of complexes C1 and C2 were inhibited by excess amounts of unlabeled NFY oligonucleotides but not with unlabeled non-specific Epstein-Barr nuclear antigen (EBNA) oligonucleotides.
To further ascertain the intrinsic Ub-binding properties, we compared the backbone dynamics of AT3-UIM12 in the presence and absence of Ub.
Furthermore, to ascertain whether the binding of ox-LDL to LOX-1 results in NF-κB activation.
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