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William R Kobertz - One of the best experts on this subject based on the ideXlab platform.

  • identification of a protein protein interaction between kcne1 and the activation gate machinery of kcnq1
    The Journal of General Physiology, 2010
    Co-Authors: Anatoli Lvov, Steven D Gage, Virla M Berrios, William R Kobertz
    Abstract:

    KCNQ1 channels assemble with KCNE1 transmembrane (TM) peptides to form voltage-gated K+ channel complexes with slow activation gate opening. The cytoplasmic C-terminal domain that abuts the KCNE1 TM segment has been implicated in regulating KCNQ1 gating, yet its interaction with KCNQ1 has not been described. Here, we identified a protein–protein interaction between the KCNE1 C-terminal domain and the KCNQ1 S6 activation gate and S4–S5 Linker. Using cysteine cross-Linking, we biochemically screened over 300 cysteine pairs in the KCNQ1–KCNE1 complex and identified three residues in KCNQ1 (H363C, P369C, and I257C) that formed disulfide bonds with cysteine residues in the KCNE1 C-terminal domain. Statistical analysis of cross-Link Efficiency showed that H363C preferentially reacted with KCNE1 residues H73C, S74C, and D76C, whereas P369C showed preference for only D76C. Electrophysiological investigation of the mutant K+ channel complexes revealed that the KCNQ1 residue, H363C, formed cross-Links not only with KCNE1 subunits, but also with neighboring KCNQ1 subunits in the complex. Cross-Link formation involving the H363C residue was state dependent, primarily occurring when the KCNQ1–KCNE1 complex was closed. Based on these biochemical and electrophysiological data, we generated a closed-state model of the KCNQ1–KCNE1 cytoplasmic region where these protein–protein interactions are poised to slow activation gate opening.

  • identification of a protein protein interaction between kcne1 and the activation gate machinery of kcnq1
    The Journal of General Physiology, 2010
    Co-Authors: Anatoli Lvov, Steven D Gage, Virla M Berrios, William R Kobertz
    Abstract:

    KCNQ1 channels assemble with KCNE1 transmembrane (TM) peptides to form voltage-gated K+ channel complexes with slow activation gate opening. The cytoplasmic C-terminal domain that abuts the KCNE1 TM segment has been implicated in regulating KCNQ1 gating, yet its interaction with KCNQ1 has not been described. Here, we identified a protein–protein interaction between the KCNE1 C-terminal domain and the KCNQ1 S6 activation gate and S4–S5 Linker. Using cysteine cross-Linking, we biochemically screened over 300 cysteine pairs in the KCNQ1–KCNE1 complex and identified three residues in KCNQ1 (H363C, P369C, and I257C) that formed disulfide bonds with cysteine residues in the KCNE1 C-terminal domain. Statistical analysis of cross-Link Efficiency showed that H363C preferentially reacted with KCNE1 residues H73C, S74C, and D76C, whereas P369C showed preference for only D76C. Electrophysiological investigation of the mutant K+ channel complexes revealed that the KCNQ1 residue, H363C, formed cross-Links not only with KCNE1 subunits, but also with neighboring KCNQ1 subunits in the complex. Cross-Link formation involving the H363C residue was state dependent, primarily occurring when the KCNQ1–KCNE1 complex was closed. Based on these biochemical and electrophysiological data, we generated a closed-state model of the KCNQ1–KCNE1 cytoplasmic region where these protein–protein interactions are poised to slow activation gate opening.

Anatoli Lvov - One of the best experts on this subject based on the ideXlab platform.

  • identification of a protein protein interaction between kcne1 and the activation gate machinery of kcnq1
    The Journal of General Physiology, 2010
    Co-Authors: Anatoli Lvov, Steven D Gage, Virla M Berrios, William R Kobertz
    Abstract:

    KCNQ1 channels assemble with KCNE1 transmembrane (TM) peptides to form voltage-gated K+ channel complexes with slow activation gate opening. The cytoplasmic C-terminal domain that abuts the KCNE1 TM segment has been implicated in regulating KCNQ1 gating, yet its interaction with KCNQ1 has not been described. Here, we identified a protein–protein interaction between the KCNE1 C-terminal domain and the KCNQ1 S6 activation gate and S4–S5 Linker. Using cysteine cross-Linking, we biochemically screened over 300 cysteine pairs in the KCNQ1–KCNE1 complex and identified three residues in KCNQ1 (H363C, P369C, and I257C) that formed disulfide bonds with cysteine residues in the KCNE1 C-terminal domain. Statistical analysis of cross-Link Efficiency showed that H363C preferentially reacted with KCNE1 residues H73C, S74C, and D76C, whereas P369C showed preference for only D76C. Electrophysiological investigation of the mutant K+ channel complexes revealed that the KCNQ1 residue, H363C, formed cross-Links not only with KCNE1 subunits, but also with neighboring KCNQ1 subunits in the complex. Cross-Link formation involving the H363C residue was state dependent, primarily occurring when the KCNQ1–KCNE1 complex was closed. Based on these biochemical and electrophysiological data, we generated a closed-state model of the KCNQ1–KCNE1 cytoplasmic region where these protein–protein interactions are poised to slow activation gate opening.

  • identification of a protein protein interaction between kcne1 and the activation gate machinery of kcnq1
    The Journal of General Physiology, 2010
    Co-Authors: Anatoli Lvov, Steven D Gage, Virla M Berrios, William R Kobertz
    Abstract:

    KCNQ1 channels assemble with KCNE1 transmembrane (TM) peptides to form voltage-gated K+ channel complexes with slow activation gate opening. The cytoplasmic C-terminal domain that abuts the KCNE1 TM segment has been implicated in regulating KCNQ1 gating, yet its interaction with KCNQ1 has not been described. Here, we identified a protein–protein interaction between the KCNE1 C-terminal domain and the KCNQ1 S6 activation gate and S4–S5 Linker. Using cysteine cross-Linking, we biochemically screened over 300 cysteine pairs in the KCNQ1–KCNE1 complex and identified three residues in KCNQ1 (H363C, P369C, and I257C) that formed disulfide bonds with cysteine residues in the KCNE1 C-terminal domain. Statistical analysis of cross-Link Efficiency showed that H363C preferentially reacted with KCNE1 residues H73C, S74C, and D76C, whereas P369C showed preference for only D76C. Electrophysiological investigation of the mutant K+ channel complexes revealed that the KCNQ1 residue, H363C, formed cross-Links not only with KCNE1 subunits, but also with neighboring KCNQ1 subunits in the complex. Cross-Link formation involving the H363C residue was state dependent, primarily occurring when the KCNQ1–KCNE1 complex was closed. Based on these biochemical and electrophysiological data, we generated a closed-state model of the KCNQ1–KCNE1 cytoplasmic region where these protein–protein interactions are poised to slow activation gate opening.

Steven D Gage - One of the best experts on this subject based on the ideXlab platform.

  • identification of a protein protein interaction between kcne1 and the activation gate machinery of kcnq1
    The Journal of General Physiology, 2010
    Co-Authors: Anatoli Lvov, Steven D Gage, Virla M Berrios, William R Kobertz
    Abstract:

    KCNQ1 channels assemble with KCNE1 transmembrane (TM) peptides to form voltage-gated K+ channel complexes with slow activation gate opening. The cytoplasmic C-terminal domain that abuts the KCNE1 TM segment has been implicated in regulating KCNQ1 gating, yet its interaction with KCNQ1 has not been described. Here, we identified a protein–protein interaction between the KCNE1 C-terminal domain and the KCNQ1 S6 activation gate and S4–S5 Linker. Using cysteine cross-Linking, we biochemically screened over 300 cysteine pairs in the KCNQ1–KCNE1 complex and identified three residues in KCNQ1 (H363C, P369C, and I257C) that formed disulfide bonds with cysteine residues in the KCNE1 C-terminal domain. Statistical analysis of cross-Link Efficiency showed that H363C preferentially reacted with KCNE1 residues H73C, S74C, and D76C, whereas P369C showed preference for only D76C. Electrophysiological investigation of the mutant K+ channel complexes revealed that the KCNQ1 residue, H363C, formed cross-Links not only with KCNE1 subunits, but also with neighboring KCNQ1 subunits in the complex. Cross-Link formation involving the H363C residue was state dependent, primarily occurring when the KCNQ1–KCNE1 complex was closed. Based on these biochemical and electrophysiological data, we generated a closed-state model of the KCNQ1–KCNE1 cytoplasmic region where these protein–protein interactions are poised to slow activation gate opening.

  • identification of a protein protein interaction between kcne1 and the activation gate machinery of kcnq1
    The Journal of General Physiology, 2010
    Co-Authors: Anatoli Lvov, Steven D Gage, Virla M Berrios, William R Kobertz
    Abstract:

    KCNQ1 channels assemble with KCNE1 transmembrane (TM) peptides to form voltage-gated K+ channel complexes with slow activation gate opening. The cytoplasmic C-terminal domain that abuts the KCNE1 TM segment has been implicated in regulating KCNQ1 gating, yet its interaction with KCNQ1 has not been described. Here, we identified a protein–protein interaction between the KCNE1 C-terminal domain and the KCNQ1 S6 activation gate and S4–S5 Linker. Using cysteine cross-Linking, we biochemically screened over 300 cysteine pairs in the KCNQ1–KCNE1 complex and identified three residues in KCNQ1 (H363C, P369C, and I257C) that formed disulfide bonds with cysteine residues in the KCNE1 C-terminal domain. Statistical analysis of cross-Link Efficiency showed that H363C preferentially reacted with KCNE1 residues H73C, S74C, and D76C, whereas P369C showed preference for only D76C. Electrophysiological investigation of the mutant K+ channel complexes revealed that the KCNQ1 residue, H363C, formed cross-Links not only with KCNE1 subunits, but also with neighboring KCNQ1 subunits in the complex. Cross-Link formation involving the H363C residue was state dependent, primarily occurring when the KCNQ1–KCNE1 complex was closed. Based on these biochemical and electrophysiological data, we generated a closed-state model of the KCNQ1–KCNE1 cytoplasmic region where these protein–protein interactions are poised to slow activation gate opening.

Virla M Berrios - One of the best experts on this subject based on the ideXlab platform.

  • identification of a protein protein interaction between kcne1 and the activation gate machinery of kcnq1
    The Journal of General Physiology, 2010
    Co-Authors: Anatoli Lvov, Steven D Gage, Virla M Berrios, William R Kobertz
    Abstract:

    KCNQ1 channels assemble with KCNE1 transmembrane (TM) peptides to form voltage-gated K+ channel complexes with slow activation gate opening. The cytoplasmic C-terminal domain that abuts the KCNE1 TM segment has been implicated in regulating KCNQ1 gating, yet its interaction with KCNQ1 has not been described. Here, we identified a protein–protein interaction between the KCNE1 C-terminal domain and the KCNQ1 S6 activation gate and S4–S5 Linker. Using cysteine cross-Linking, we biochemically screened over 300 cysteine pairs in the KCNQ1–KCNE1 complex and identified three residues in KCNQ1 (H363C, P369C, and I257C) that formed disulfide bonds with cysteine residues in the KCNE1 C-terminal domain. Statistical analysis of cross-Link Efficiency showed that H363C preferentially reacted with KCNE1 residues H73C, S74C, and D76C, whereas P369C showed preference for only D76C. Electrophysiological investigation of the mutant K+ channel complexes revealed that the KCNQ1 residue, H363C, formed cross-Links not only with KCNE1 subunits, but also with neighboring KCNQ1 subunits in the complex. Cross-Link formation involving the H363C residue was state dependent, primarily occurring when the KCNQ1–KCNE1 complex was closed. Based on these biochemical and electrophysiological data, we generated a closed-state model of the KCNQ1–KCNE1 cytoplasmic region where these protein–protein interactions are poised to slow activation gate opening.

  • identification of a protein protein interaction between kcne1 and the activation gate machinery of kcnq1
    The Journal of General Physiology, 2010
    Co-Authors: Anatoli Lvov, Steven D Gage, Virla M Berrios, William R Kobertz
    Abstract:

    KCNQ1 channels assemble with KCNE1 transmembrane (TM) peptides to form voltage-gated K+ channel complexes with slow activation gate opening. The cytoplasmic C-terminal domain that abuts the KCNE1 TM segment has been implicated in regulating KCNQ1 gating, yet its interaction with KCNQ1 has not been described. Here, we identified a protein–protein interaction between the KCNE1 C-terminal domain and the KCNQ1 S6 activation gate and S4–S5 Linker. Using cysteine cross-Linking, we biochemically screened over 300 cysteine pairs in the KCNQ1–KCNE1 complex and identified three residues in KCNQ1 (H363C, P369C, and I257C) that formed disulfide bonds with cysteine residues in the KCNE1 C-terminal domain. Statistical analysis of cross-Link Efficiency showed that H363C preferentially reacted with KCNE1 residues H73C, S74C, and D76C, whereas P369C showed preference for only D76C. Electrophysiological investigation of the mutant K+ channel complexes revealed that the KCNQ1 residue, H363C, formed cross-Links not only with KCNE1 subunits, but also with neighboring KCNQ1 subunits in the complex. Cross-Link formation involving the H363C residue was state dependent, primarily occurring when the KCNQ1–KCNE1 complex was closed. Based on these biochemical and electrophysiological data, we generated a closed-state model of the KCNQ1–KCNE1 cytoplasmic region where these protein–protein interactions are poised to slow activation gate opening.

Paul D Mitcheson - One of the best experts on this subject based on the ideXlab platform.

  • Link Efficiency led design of mid range inductive power transfer systems
    2015 IEEE PELS Workshop on Emerging Technologies: Wireless Power (2015 WoW), 2015
    Co-Authors: Christopher H Kwan, George Kkelis, Samer Aldhaher, James R Lawson, David C Yates, P C K Luk, Paul D Mitcheson
    Abstract:

    For mid-range inductive power transfer (IPT) systems, improving Link Efficiency entails operating in the multi-MHz region in order to increase coil Q factors. However, designing end-to-end systems at such frequencies poses challenges associated with the Efficiency of the power electronics. This paper presents a set of design principles with the aim of achieving maximal DC-to-load Efficiency of such systems. These include the selection of semiconductor devices and power converter topologies that are suitable for high frequencies. Through these design methods, a 6.78MHz ISM-band IPT system has been implemented, transferring 120W of power across 30 cm with a DC-to-load Efficiency of ∼70 %.

  • maximizing dc to load Efficiency for inductive power transfer
    IEEE Transactions on Power Electronics, 2013
    Co-Authors: M Pinuela, David C Yates, S Lucyszyn, Paul D Mitcheson
    Abstract:

    Inductive power transfer (IPT) systems for transmitting tens to hundreds of watts have been reported for almost a decade. Most of the work has concentrated on the optimization of the Link Efficiency and has not taken into account the Efficiency of the driver. Class-E amplifiers have been identified as ideal drivers for IPT applications, but their power handling capability at tens of megahertz has been a crucial limiting factor, since the load and inductor characteristics are set by the requirements of the resonant inductive system. The frequency limitation of the driver restricts the unloaded Q-factor of the coils and thus the Link Efficiency. With a suitable driver, copper coil unloaded Q factors of over 1000 can be achieved in the low megahertz region, enabling a cost-effective high Q coil assembly. The system presented in this paper alleviates the use of heavy and expensive field-shaping techniques by presenting an efficient IPT system capable of transmitting energy with a dc-to-load Efficiency above 77% at 6 MHz across a distance of 30 cm. To the authors knowledge, this is the highest dc-to-load Efficiency achieved for an IPT system without introducing restrictive coupling factor enhancement techniques.