@inbook{4a902fc59efc4c1392d4d8fb79605cf5,
title = "Nuclear magnetic resonance approaches for characterizing protein-protein interactions",
abstract = "The gating of potassium ion (K+) channels is regulated by various kinds of protein-protein interactions (PPIs). Structural investigations of these PPIs provide useful information not only for understanding the gating mechanisms of K+ channels, but also for developing the pharmaceutical compounds targeting K+ channels. Here, we describe a nuclear magnetic resonance spectroscopic method, termed the cross saturation (CS) method, to accurately determine the binding surfaces of protein complexes, and its application to the investigation of the interaction between a G protein-coupled inwardly rectifying K+ channel and a G protein α subunit.",
keywords = "Cross saturation, G protein, GIRK, NMR, Protein-protein interaction",
author = "Yuki Toyama and Yoko Mase and Hanaho Kano and Mariko Yokogawa and Masanori Osawa and Ichio Shimada",
note = "Publisher Copyright: {\textcopyright} 2018, Springer Science+Business Media LLC.",
year = "2018",
doi = "10.1007/978-1-4939-7362-0_10",
language = "English",
series = "Methods in Molecular Biology",
publisher = "Humana Press Inc.",
pages = "115--128",
booktitle = "Methods in Molecular Biology",
}