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Based on structural information for a peptide (P8-2KAQ) that binds to granulocyte-colony stimulating factor receptor (G-CSFR), small ligands with a biaryl scaffold were designed and their binding affinities were evaluated.
The binding affinities were evaluated over a range of 2.5 40 mmol/L concentrations.
ER binding affinities were evaluated by a fluorescent polarization assay with the corresponding inactive In III) complex or iodinated peptide.
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The peptide binding affinity was evaluated for each variant using different protein concentrations (from 20 nM to 500 μM) with a constant concentration of fluorescent peptide (100 nM) in a reaction volume of 20 μL.
This affinity is evaluated in dose response curves which, showed a dose -dependent increase in binding that reflects the affinity the peptides confer to the particles.
Region-specific binding affinities were analyzed using Student's unpaired t-test.
Linear correlations between the predicted binding scores and the experimentally measured binding affinities were observed.
The correlation between PharmDock's predicted binding energies with the experimentally measured binding affinities was used to evaluate PharmDock's performance in binding energy estimation.
Moreover, the binding affinities and selectivity were evaluated via fluorescence polarization (FP) assay.
Bivalent ligands constituted by two identical pharmacophores structurally related to the Nociceptin Opioid Receptor (NOPr) antagonist JTC-801 were synthesized and their binding affinities for NOPr were evaluated.
With the formation of ligand protein complex, binding affinity can be evaluated by monitoring the heat that quantitatively occurs in the release and absorption of the binding process [158, 159].
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