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As predicted, two of the representative C-7α-substituted derivatives of E2 synthesized in the present study retained strong binding affinities (close to those of E2 and ICI-182,780) for the human ERα and ERβ subtypes as determined using the radioligand receptor binding assays.
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The W187Y mutant is able to bind CPSF30 with a binding affinity close to the wild-type protein; that is, it retains a receptor site for aromatic ligands nearly identical to the wild-type.
We have recently provided evidence that specific OB receptors are present in ventricular myocardial cells [ 18], with a receptor density and binding affinity quite close to those previously found in rodent and human pancreatic β-cells, where OB promotes cell survival and induces expression of genes involved in the regulation of β-cell mass and function [ 10, 11].
But on the other hand, particularly for small populations, where the common ancestor binding energy distribution is broad, there will be common ancestor gene pairs, whose binding affinity is closer to the inviability boundary, which would tend to dominate t *, giving a t * that is shorter than our estimate.
Since our DRT reference set mainly focuses on strong binders to a specific protein, the low rankings of the target for these two drugs may be partially attributed to their low binding affinities to the target, which are close to the threshold for selecting ligands in our reference set.
This means that in direct ligand competition assays with Fl-E2, the compound should be able to compete with the fluorescently labelled E2 and its binding affinity should be close to 1/5,800th that of E2.
These mSlo1/β4 mutant channels also display higher binding affinities to ChTX than mSlo1/β4 channel.
c Bar chart showing the binding affinities of bBest2 to ATP analogs.
As shown in Table 2, all these channels present higher binding affinities to ChTX than mSlo1/β4 channel does.
For all ligands studied, there were multiple pairs of CR domains, all taken from cluster II of LRP, that could generate a binding site with affinity very close to that reported for the ligand to intact LRP.
Biotinylated M1, M2, or M1 + M2 LoNA (mutations on LoNA NCL-binding sites) showed no preferential binding affinity to FBL as compared to WT LoNA (Supplementary Fig. 4c).
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