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

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.

Original languageEnglish
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Pages115-128
Number of pages14
Volume1684
DOIs
Publication statusPublished - 2018

Publication series

NameMethods in Molecular Biology
Volume1684
ISSN (Print)1064-3745

Keywords

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

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

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  • Cite this

    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). (Methods in Molecular Biology; Vol. 1684). Humana Press Inc.. https://doi.org/10.1007/978-1-4939-7362-0_10