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Here, we have investigated the relationships between physicochemical properties, binding kinetics and functional activity in two different signal transduction pathways, G protein activation and β-arrestin recruitment.
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To understand whether the duplicated IGFBP-1 genes have evolved distinct structural and functional properties, we have investigated their spatial and temporal expression, physiological regulation, IGF binding kinetics, and biological activities.
At the receiver, we consider two different configurations of molecular antenna kinetics, the surface receptor-ligand binding kinetics, and the enzyme-catalyzed reaction kinetics.
Hence, the reception mechanism of the receiver is modeled separately as ligand-receptor binding kinetics and as enzyme-catalyzed biochemical reaction kinetics.
Secondly, the grafting density of these films can be tuned to optimize binding kinetics and capacity.
To determine how rapidly the effect of ligand-induced changes in dimerization kinetics can result in receptor re-organization on the membrane, MC simulations were run for different concentrations of ligand, receptor/ligand binding kinetics, and dimerization kinetics.
In addition, peptides have minimal immunogenicity and can exhibit rapid binding kinetics and diffuse into diseased mucosa.
To determine the binding kinetics and affinity we performed an SPR-based assay on a BIAcore 3000.
The binding kinetics and affinities were determined by globally fitting the curves of 5 concentrations to a 1∶1 Langmuir model.
This method was used to study binding kinetics and enzyme activity.
Microfluidic integrated nanohole arrays have been used for analyzing antibody ligand binding kinetics and biomarkers.
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