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The results proved that both compounds adopt a similar architecture.
These compounds adopt a trigonal bipyramidal structure in which the lone pair always occupies an equatorial position.
X-ray crystallography revealed that these compounds adopt a bioactive conformation, in the kinase domain, consistent with that previously seen with 2-pyridone-based Met kinase inhibitors.
Molecular docking of compounds 1 3 with α-glucosidase and α-amylase predicted that these compounds adopt a similar conformation and bind in similar site as acarbose.
12 Nevertheless, it is likely that our compounds adopt a broadly similar orientation to tropisetron; therefore, the models serve as means of identifying residues that could potentially be responsible for the differences in affinities of the quinoxaline ligands at 5-HT3A and 5-HT3AB receptors.
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The 1H and 13C NMR spectra indicate that these compounds adopt an anti-(E) conformation in solution, and confirmed for 1b by the X-ray crystal crystallography.
Furthermore, limited cross-resistance was observed for decoquinate against ATQ-R lines,which supports the molecular model that each of these compounds adopts a different mode of binding within the ubiquinol-binding site of PfCYT b.
The 1H and 13C NMR spectra indicated that these compounds adopted an anti-(E) conformation in solution, and this was confirmed by X-ray crystallography for one of the complexes (NT2).
Interestingly, docking studies of the N4 4-methoxyphenyl derivatives (43, 48, 52 and 54– 56) showed that most of the compounds adopted an alternative binding pose compared to that of the N4 furfuryl compounds (Fig. 2c).
One inhibitor presented here exhibits no PKB/PKA selectivity, and the compound adopts a similar binding mode in all three systems.
At temperatures of 400 450 °C, technetium oxidizes to form the pale-yellow heptoxide: : 4 Tc + 7 O2 → 2 This7 This compound adopts a centrosymmetric structure with two types of Tc-O bonds; their bond lengths are 167 and 184 pm, and the O-Tc-O angle is 180°.
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