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.
CITATION STYLE
Toyama, Y., Mase, Y., Kano, H., Yokogawa, M., Osawa, M., & Shimada, I. (2018). Nuclear magnetic resonance approaches for characterizing protein-protein interactions. In Methods in Molecular Biology (Vol. 1684, pp. 115–128). Humana Press Inc. https://doi.org/10.1007/978-1-4939-7362-0_10
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