Chapter title |
Nuclear Magnetic Resonance Approaches for Characterizing Protein-Protein Interactions
|
---|---|
Chapter number | 10 |
Book title |
Potassium Channels
|
Published in |
Methods in molecular biology, January 2018
|
DOI | 10.1007/978-1-4939-7362-0_10 |
Pubmed ID | |
Book ISBNs |
978-1-4939-7361-3, 978-1-4939-7362-0
|
Authors |
Yuki Toyama, Yoko Mase, Hanaho Kano, Mariko Yokogawa, Masanori Osawa, Ichio Shimada |
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. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
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Unknown | 5 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
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Researcher | 2 | 40% |
Student > Ph. D. Student | 1 | 20% |
Other | 1 | 20% |
Unknown | 1 | 20% |
Readers by discipline | Count | As % |
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Biochemistry, Genetics and Molecular Biology | 3 | 60% |
Unknown | 2 | 40% |