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Binding affinity can exert a significant influence on both the equilibrium and the dynamic response characteristics of such a biosensor.
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This relative binding affinity can then be compared with R values extracted from other images.
DNA binding modes and binding affinity can be modulated by ligand design.
We show that type II binding can have a profound influence on binding affinity for CYP3A4, and the difference in binding affinity can be as high as 1200-fold.
Based on these, energetically favorable and unfavorable contributions to the binding affinity can be assessed on an atomic level.
Biochemical assays of binding affinity can be developed into a high-throughput screen.
Our results suggest that aptamers with broad AMG binding affinity can be isolated by this route.
The relative binding affinities can be simultaneously determined.
The binding affinities can vary by several orders of magnitude [ 13].
These binding sites may have low sequence specificities, but their binding affinities can be complemented by high structure specificities.
The binding affinities can be compared to the affinity constants determined for MBP from the association and dissociation rates (kon/ koff) and measured with stopped-flow fluorescence spectroscopy.
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