Voltage sensor gating charge transfer in a HERG potassium channel model

Charlotte K Colenso; Yang Cao; Richard B Sessions; Jules C Hancox; Christopher E Dempsey

doi:10.1016/j.bpj.2014.10.001

Voltage sensor gating charge transfer in a HERG potassium channel model

Charlotte K Colenso, Yang Cao, Richard B Sessions, Jules C Hancox, Christopher E Dempsey

Research output: Contribution to journal › Article (Academic Journal) › peer-review

3 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	L25-8
Journal	Biophysical Journal
Volume	107
Issue number	10
DOIs	https://doi.org/10.1016/j.bpj.2014.10.001
Publication status	Published - 18 Nov 2014

Research Groups and Themes

Bristol BioDesign Institute

Keywords

synthetic biology

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10.1016/j.bpj.2014.10.001

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Cite this

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title = "Voltage sensor gating charge transfer in a HERG potassium channel model",

abstract = "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.",

keywords = "synthetic biology",

author = "Colenso, \{Charlotte K\} and Yang Cao and Sessions, \{Richard B\} and Hancox, \{Jules C\} and Dempsey, \{Christopher E\}",

year = "2014",

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doi = "10.1016/j.bpj.2014.10.001",

language = "English",

volume = "107",

pages = "L25--8",

journal = "Biophysical Journal",

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TY - JOUR

T1 - Voltage sensor gating charge transfer in a HERG potassium channel model

AU - Colenso, Charlotte K

AU - Cao, Yang

AU - Sessions, Richard B

AU - Hancox, Jules C

AU - Dempsey, Christopher E

PY - 2014/11/18

Y1 - 2014/11/18

N2 - 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.

AB - 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.

KW - synthetic biology

U2 - 10.1016/j.bpj.2014.10.001

DO - 10.1016/j.bpj.2014.10.001

M3 - Article (Academic Journal)

C2 - 25418316

SN - 0006-3495

VL - 107

SP - L25-8

JO - Biophysical Journal

JF - Biophysical Journal

IS - 10

ER -