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Thermodynamics of voltage-gated ion channels
Ion channels are essential for cellular signaling. Voltage-gated ion channels (VGICs) are the largest and most extensively studied superfamily of ion channels. They possess modular structural features such as voltage-sensing domains that encircle and form mechanical connections with the pore-forming...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Berlin Heidelberg
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6276078/ https://www.ncbi.nlm.nih.gov/pubmed/30596139 http://dx.doi.org/10.1007/s41048-018-0074-y |
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author | Zhang, Xuejun C. Yang, Hanting Liu, Zhenfeng Sun, Fei |
author_facet | Zhang, Xuejun C. Yang, Hanting Liu, Zhenfeng Sun, Fei |
author_sort | Zhang, Xuejun C. |
collection | PubMed |
description | Ion channels are essential for cellular signaling. Voltage-gated ion channels (VGICs) are the largest and most extensively studied superfamily of ion channels. They possess modular structural features such as voltage-sensing domains that encircle and form mechanical connections with the pore-forming domains. Such features are intimately related to their function in sensing and responding to changes in the membrane potential. In the present work, we discuss the thermodynamic mechanisms of the VGIC superfamily, including the two-state gating mechanism, sliding-rocking mechanism of the voltage sensor, subunit cooperation, lipid-infiltration mechanism of inactivation, and the relationship with their structural features. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s41048-018-0074-y) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-6276078 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
spelling | pubmed-62760782018-12-26 Thermodynamics of voltage-gated ion channels Zhang, Xuejun C. Yang, Hanting Liu, Zhenfeng Sun, Fei Biophys Rep Review Ion channels are essential for cellular signaling. Voltage-gated ion channels (VGICs) are the largest and most extensively studied superfamily of ion channels. They possess modular structural features such as voltage-sensing domains that encircle and form mechanical connections with the pore-forming domains. Such features are intimately related to their function in sensing and responding to changes in the membrane potential. In the present work, we discuss the thermodynamic mechanisms of the VGIC superfamily, including the two-state gating mechanism, sliding-rocking mechanism of the voltage sensor, subunit cooperation, lipid-infiltration mechanism of inactivation, and the relationship with their structural features. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s41048-018-0074-y) contains supplementary material, which is available to authorized users. Springer Berlin Heidelberg 2018-11-16 2018 /pmc/articles/PMC6276078/ /pubmed/30596139 http://dx.doi.org/10.1007/s41048-018-0074-y Text en © The Author(s) 2018 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
spellingShingle | Review Zhang, Xuejun C. Yang, Hanting Liu, Zhenfeng Sun, Fei Thermodynamics of voltage-gated ion channels |
title | Thermodynamics of voltage-gated ion channels |
title_full | Thermodynamics of voltage-gated ion channels |
title_fullStr | Thermodynamics of voltage-gated ion channels |
title_full_unstemmed | Thermodynamics of voltage-gated ion channels |
title_short | Thermodynamics of voltage-gated ion channels |
title_sort | thermodynamics of voltage-gated ion channels |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6276078/ https://www.ncbi.nlm.nih.gov/pubmed/30596139 http://dx.doi.org/10.1007/s41048-018-0074-y |
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