<div><p>Biolayer interferometry is a method to analyze protein interactions in real-time. In this study, we illustrate the usefulness to quantitatively analyze high affinity protein ligand interactions employing a kinetic titration series for characterizing the interactions between two pairs of interaction patterns, in particular immunoglobulin G and protein G B1 as well as scFv IC16 and amyloid beta (1–42). Kinetic titration series are commonly used in surface plasmon resonance and involve sequential injections of analyte over a desired concentration range on a single ligand coated sensor chip without waiting for complete dissociation between the injections. We show that applying this method to biolayer interferometry is straightforward an...
The interaction between membrane proteins and their (protein) ligands is conventionally investigated...
Binding affinity of biomolecular interactions can be directly extracted from measured surface plasmo...
The values of the affinity constants (kd, ka, and KD) that are determined by label-free interaction ...
Biolayer interferometry is a method to analyze protein interactions in real-time. In this study, we ...
Biolayer interferometry is a method to analyze protein interactions in real-time. In this study, we ...
Biolayer interferometry (BLI) is an emerging analytical tool that allows the study of protein comple...
An undergraduate biochemistry laboratory experiment has been developed using biolayer interferometry...
In this paper we show a high-throughput method to screen the kinetics and affinity constants of many...
<p>A. Biolayer interferometry analysis of peptides with APPs. Biotinylated peptides were immobilized...
Kinetic analysis of biomolecular interactions are powerfully used to quantify the binding kinetic co...
Biologics are pharmaceutical drug products whose active drug substance is produced in a living organ...
Biolayer interferometry (BLI) is a widely utilized technique for determining macromolecular interact...
An undergraduate biochemistry laboratory experiment has been developed using biolayer interferometr...
A procedure for evaluating the thermodynamic equilibrium constant by kinetic analysis of sensorgrams...
Kinetic monitoring of protein-protein interactions offers fundamental insights of their cellular fun...
The interaction between membrane proteins and their (protein) ligands is conventionally investigated...
Binding affinity of biomolecular interactions can be directly extracted from measured surface plasmo...
The values of the affinity constants (kd, ka, and KD) that are determined by label-free interaction ...
Biolayer interferometry is a method to analyze protein interactions in real-time. In this study, we ...
Biolayer interferometry is a method to analyze protein interactions in real-time. In this study, we ...
Biolayer interferometry (BLI) is an emerging analytical tool that allows the study of protein comple...
An undergraduate biochemistry laboratory experiment has been developed using biolayer interferometry...
In this paper we show a high-throughput method to screen the kinetics and affinity constants of many...
<p>A. Biolayer interferometry analysis of peptides with APPs. Biotinylated peptides were immobilized...
Kinetic analysis of biomolecular interactions are powerfully used to quantify the binding kinetic co...
Biologics are pharmaceutical drug products whose active drug substance is produced in a living organ...
Biolayer interferometry (BLI) is a widely utilized technique for determining macromolecular interact...
An undergraduate biochemistry laboratory experiment has been developed using biolayer interferometr...
A procedure for evaluating the thermodynamic equilibrium constant by kinetic analysis of sensorgrams...
Kinetic monitoring of protein-protein interactions offers fundamental insights of their cellular fun...
The interaction between membrane proteins and their (protein) ligands is conventionally investigated...
Binding affinity of biomolecular interactions can be directly extracted from measured surface plasmo...
The values of the affinity constants (kd, ka, and KD) that are determined by label-free interaction ...