Measuring the KD of Protein-Ligand Interactions Using Microscale Thermophoresis.
Methods Mol Biol
; 2263: 161-181, 2021.
Article
in En
| MEDLINE
| ID: mdl-33877597
ABSTRACT
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.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Glycine max
/
Chymotrypsin
/
Trypsin Inhibitors
Limits:
Animals
/
Humans
Language:
En
Journal:
Methods Mol Biol
Journal subject:
BIOLOGIA MOLECULAR
Year:
2021
Document type:
Article
Affiliation country:
United States