Probing the interaction of the potassium channel modulating KCNE1 in lipid bilayers via solid‐state NMR spectroscopy
Author:
Affiliation:
1. Cell, Molecular, and Structural Biology Graduate Program Miami University Oxford OH 45056 USA
2. Department of Chemistry and Biochemistry Miami University Oxford OH 45056 USA
Funder
Division of Chemistry
National Institute of General Medical Sciences
Publisher
Wiley
Subject
General Materials Science,General Chemistry
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/mrc.4589
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1. The MinK-related peptides
2. KvLQT1 and IsK (minK) proteins associate to form the IKS cardiac potassium current
3. Coassembly of KVLQT1 and minK (IsK) proteins to form cardiac IKS potassium channel
4. Disease‐associated mutations in KCNE potassium channel subunits (MiRPs) reveal promiscuous disruption of multiple currents and conservation of mechanism
5. KCNQ1 Gain-of-Function Mutation in Familial Atrial Fibrillation
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1. Probing the Dynamics and Structural Topology of the Reconstituted Human KCNQ1 Voltage Sensor Domain (Q1-VSD) in Lipid Bilayers Using Electron Paramagnetic Resonance Spectroscopy;Biochemistry;2019-01-08
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