Using two-site binding models to analyze microscale thermophoresis data

The emergence of microscale thermophoresis (MST) as a technique for determining the dissociation constants for bimolecular interactions has enabled these quantities to be measured in systems that were previously difficult or impracticable. However, most models for analyses of these data featured the...

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Veröffentlicht in:	Analytical biochemistry 2018-01, Vol.540-541, p.64-75
Hauptverfasser:	Tso, Shih-Chia, Chen, Qiuyan, Vishnivetskiy, Sergey A., Gurevich, Vsevolod V., Iverson, T.M., Brautigam, Chad A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Monophosphate - chemistry Adenosine Monophosphate - metabolism Algorithms Animals Aptamers, Nucleotide - chemistry Aptamers, Nucleotide - genetics Aptamers, Nucleotide - metabolism Arrestin-3 beta-Arrestin 2 - chemistry beta-Arrestin 2 - metabolism Binding Sites Cattle DNA aptamer Kinetics Microscale thermophoresis Models, Molecular Monte Carlo Method Mutagenesis, Site-Directed Phytic Acid - chemistry Phytic Acid - metabolism Protein Binding Protein-ligand interactions Protein-protein interactions Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification
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