Nuclear magnetic resonance approaches for characterizing protein-protein interactions

Yuki Toyama, Yoko Mase, Hanaho Kano, Mariko Yokogawa, Masanori Osawa, Ichio Shimada

Research output: Chapter in Book/Report/Conference proceedingChapter


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.

Original languageEnglish
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Number of pages14
Publication statusPublished - 2018

Publication series

NameMethods in Molecular Biology
ISSN (Print)1064-3745


  • Cross saturation
  • G protein
  • GIRK
  • NMR
  • Protein-protein interaction

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics


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