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The binding models were determined using HT-SELEX, the same method we have used previously to determine specificities of mammalian TFs.
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Subsequently a one-site binding model was determined as the appropriate form of analysis for all binding data.
The data were analyzed with ProteON Manager™ 3.1 software (Bio-Rad, Hercules, CA, USA), and binding constants were determined using a 1 1 Langmuir binding model.
In this paper, the inhibitory kinetics of glabridin on tyrosinase and their binding mechanisms were determined using spectroscopic, zebrafish model and molecular docking techniques.
The data were analyzed with the ProteON Manager TM 2.1 software; binding constants were determined using the software's Langmuir model.
The binding strength and the number of binding sites were determined at different ionic strengths.
The binding parameters were determined by fluorescence anisotropy measurements.
In vitro GRPR-binding affinities were determined with competitive binding assays on PC3 human prostate cancer cells.
The binding kinetics and affinities were determined by globally fitting the curves of 5 concentrations to a 1∶1 Langmuir model.
Stability, protein binding and logP values were determined.
The locations and a general ligand binding interaction model for the LBS were determined, leading to the discovery of novel mitoNEET ligands.
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