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Analysis of binding by thermophoresis revealed that in contrast to full-length BiP, we measured no binding between luminal domains and BiP's substrate binding domain.
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Rapid mixing experiments measuring NO binding to the ferric protein were conducted with a BioLogic SFM 400 stopped-flow reactor coupled to a MOS 250 spectrophotometer.
First attempts to measure ferric NO binding displayed non-saturated spectrum at low NO concentrations.
(B ) Approximate on- and off-rates of IRES-ribosome binding measured by filter binding.
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.
A2A and A2B AR equilibrium binding parameters were measured using radioligand binding assays.
The CDN measured protein binding was 86.9%.
Linear correlations between the predicted binding scores and the experimentally measured binding affinities were observed.
Figure 7 shows the correlations between the experimentally measured binding constants (in –log Kd units) and the predicted binding scores by PharmDock for all tested protein-ligand complexes.
Another important evaluation of the docking program is how well the predicted binding energies correlate with the experimentally measured binding affinities.
Figure 7 Correlations between the experimentally measured binding constants of the protein-ligand complexes and the PharmDock-predicted binding scores.
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