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Voltage Sensor Gating Charge Transfer in a hERG Potassium Channel Model

Relaxation of a hERG K(+) channel model during molecular-dynamics simulation in a hydrated POPC bilayer was accompanied by transitions of an arginine gating charge across a charge transfer center in two voltage sensor domains. Inspection of the passage of arginine side chains across the charge trans...

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Autores principales: Colenso, Charlotte K., Cao, Yang, Sessions, Richard B., Hancox, Jules C., Dempsey, Christopher E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Biophysical Society 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4241455/
https://www.ncbi.nlm.nih.gov/pubmed/25418316
http://dx.doi.org/10.1016/j.bpj.2014.10.001
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author Colenso, Charlotte K.
Cao, Yang
Sessions, Richard B.
Hancox, Jules C.
Dempsey, Christopher E.
author_facet Colenso, Charlotte K.
Cao, Yang
Sessions, Richard B.
Hancox, Jules C.
Dempsey, Christopher E.
author_sort Colenso, Charlotte K.
collection PubMed
description Relaxation of a hERG K(+) channel model during molecular-dynamics simulation in a hydrated POPC bilayer was accompanied by transitions of an arginine gating charge across a charge transfer center in two voltage sensor domains. Inspection of the passage of arginine side chains across the charge transfer center suggests that the unique hydration properties of the arginine guanidine cation facilitates charge transfer during voltage sensor responses to changes in membrane potential, and underlies the preference of Arg over Lys as a mobile charge carrier in voltage-sensitive ion channels.
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spelling pubmed-42414552015-07-16 Voltage Sensor Gating Charge Transfer in a hERG Potassium Channel Model Colenso, Charlotte K. Cao, Yang Sessions, Richard B. Hancox, Jules C. Dempsey, Christopher E. Biophys J Biophysical Letter Relaxation of a hERG K(+) channel model during molecular-dynamics simulation in a hydrated POPC bilayer was accompanied by transitions of an arginine gating charge across a charge transfer center in two voltage sensor domains. Inspection of the passage of arginine side chains across the charge transfer center suggests that the unique hydration properties of the arginine guanidine cation facilitates charge transfer during voltage sensor responses to changes in membrane potential, and underlies the preference of Arg over Lys as a mobile charge carrier in voltage-sensitive ion channels. The Biophysical Society 2014-11-18 /pmc/articles/PMC4241455/ /pubmed/25418316 http://dx.doi.org/10.1016/j.bpj.2014.10.001 Text en © 2014 The Authors http://creativecommons.org/licenses/by/3.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Biophysical Letter
Colenso, Charlotte K.
Cao, Yang
Sessions, Richard B.
Hancox, Jules C.
Dempsey, Christopher E.
Voltage Sensor Gating Charge Transfer in a hERG Potassium Channel Model
title Voltage Sensor Gating Charge Transfer in a hERG Potassium Channel Model
title_full Voltage Sensor Gating Charge Transfer in a hERG Potassium Channel Model
title_fullStr Voltage Sensor Gating Charge Transfer in a hERG Potassium Channel Model
title_full_unstemmed Voltage Sensor Gating Charge Transfer in a hERG Potassium Channel Model
title_short Voltage Sensor Gating Charge Transfer in a hERG Potassium Channel Model
title_sort voltage sensor gating charge transfer in a herg potassium channel model
topic Biophysical Letter
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4241455/
https://www.ncbi.nlm.nih.gov/pubmed/25418316
http://dx.doi.org/10.1016/j.bpj.2014.10.001
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