Measuring the KD of Protein-Ligand Interactions Using Microscale Thermophoresis.
Methods Mol Biol
; 2263: 161-181, 2021.
Article
em En
| MEDLINE
| ID: mdl-33877597
Microscale thermophoresis (MST) has become a widely used technique to determine the KD or EC50 of protein-ligand interactions. The method exploits the tendency of macromolecules to migrate along a thermal gradient (i.e., thermophoresis). Differences in thermophoresis as a function of the liganded state of a macromolecule can be measured and assembled into a binding curve that can be analyzed to yield KD. In this protocol, we outline a simple experiment designed for new MST users, with the goal of using readily available, inexpensive materials to plan, execute, and analyze an MST experiment.
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01-internacional
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MEDLINE
Assunto principal:
Glycine max
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Quimotripsina
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Inibidores da Tripsina
Limite:
Animals
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Humans
Idioma:
En
Ano de publicação:
2021
Tipo de documento:
Article