@inbook{1f1f97defc7945fda994c32a5d696684,
title = "Measuring the KD of Protein–Ligand Interactions Using Microscale Thermophoresis",
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.",
keywords = "Affinity measurement, K, Microscale thermophoresis, Protein–ligand interactions, Protein–protein interactions",
author = "Tso, {Shih Chia} and Brautigam, {Chad A.}",
note = "Publisher Copyright: {\textcopyright} 2021, Springer Science+Business Media, LLC, part of Springer Nature.",
year = "2021",
doi = "10.1007/978-1-0716-1197-5_6",
language = "English (US)",
series = "Methods in Molecular Biology",
publisher = "Humana Press Inc.",
pages = "161--181",
booktitle = "Methods in Molecular Biology",
}