A theoretical model for calculating voltage sensitivity of ion channels and the application on Kv1.2 potassium channel

Huaiyu Yang, Zhaobing Gao, Ping Li, Kunqian Yu, Ye Yu, Tian Le Xu, Min Li, Hualiang Jiang

Research output: Contribution to journalArticle

Abstract

Voltage sensing confers conversion of a change in membrane potential to signaling activities underlying the physiological processes. For an ion channel, voltage sensitivity is usually experimentally measured by fitting electrophysiological data to Boltzmann distributions. In our study, a two-state model of the ion channel and equilibrium statistical mechanics principle were used to test the hypothesis of empirically calculating the overall voltage sensitivity of an ion channel on the basis of its closed and open conformations, and determine the contribution of individual residues to the voltage sensing. We examined the theoretical paradigm by performing experimental measurements with Kv1.2 channel and a series of mutants. The correlation between the calculated values and the experimental values is at respective level, R 2 = 0.73. Our report therefore provides in silico prediction of key conformations and has identified additional residues critical for voltage sensing.

Original languageEnglish (US)
Pages (from-to)1815-1825
Number of pages11
JournalBiophysical Journal
Volume102
Issue number8
DOIs
StatePublished - Apr 18 2012

Fingerprint

Kv1.2 Potassium Channel
Ion Channels
Theoretical Models
Physiological Phenomena
Mechanics
Computer Simulation
Membrane Potentials

ASJC Scopus subject areas

  • Biophysics

Cite this

A theoretical model for calculating voltage sensitivity of ion channels and the application on Kv1.2 potassium channel. / Yang, Huaiyu; Gao, Zhaobing; Li, Ping; Yu, Kunqian; Yu, Ye; Xu, Tian Le; Li, Min; Jiang, Hualiang.

In: Biophysical Journal, Vol. 102, No. 8, 18.04.2012, p. 1815-1825.

Research output: Contribution to journalArticle

Yang, Huaiyu ; Gao, Zhaobing ; Li, Ping ; Yu, Kunqian ; Yu, Ye ; Xu, Tian Le ; Li, Min ; Jiang, Hualiang. / A theoretical model for calculating voltage sensitivity of ion channels and the application on Kv1.2 potassium channel. In: Biophysical Journal. 2012 ; Vol. 102, No. 8. pp. 1815-1825.
@article{0d474df90ab349698e2df41bc2f48022,
title = "A theoretical model for calculating voltage sensitivity of ion channels and the application on Kv1.2 potassium channel",
abstract = "Voltage sensing confers conversion of a change in membrane potential to signaling activities underlying the physiological processes. For an ion channel, voltage sensitivity is usually experimentally measured by fitting electrophysiological data to Boltzmann distributions. In our study, a two-state model of the ion channel and equilibrium statistical mechanics principle were used to test the hypothesis of empirically calculating the overall voltage sensitivity of an ion channel on the basis of its closed and open conformations, and determine the contribution of individual residues to the voltage sensing. We examined the theoretical paradigm by performing experimental measurements with Kv1.2 channel and a series of mutants. The correlation between the calculated values and the experimental values is at respective level, R 2 = 0.73. Our report therefore provides in silico prediction of key conformations and has identified additional residues critical for voltage sensing.",
author = "Huaiyu Yang and Zhaobing Gao and Ping Li and Kunqian Yu and Ye Yu and Xu, {Tian Le} and Min Li and Hualiang Jiang",
year = "2012",
month = "4",
day = "18",
doi = "10.1016/j.bpj.2012.03.032",
language = "English (US)",
volume = "102",
pages = "1815--1825",
journal = "Biophysical Journal",
issn = "0006-3495",
publisher = "Biophysical Society",
number = "8",

}

TY - JOUR

T1 - A theoretical model for calculating voltage sensitivity of ion channels and the application on Kv1.2 potassium channel

AU - Yang, Huaiyu

AU - Gao, Zhaobing

AU - Li, Ping

AU - Yu, Kunqian

AU - Yu, Ye

AU - Xu, Tian Le

AU - Li, Min

AU - Jiang, Hualiang

PY - 2012/4/18

Y1 - 2012/4/18

N2 - Voltage sensing confers conversion of a change in membrane potential to signaling activities underlying the physiological processes. For an ion channel, voltage sensitivity is usually experimentally measured by fitting electrophysiological data to Boltzmann distributions. In our study, a two-state model of the ion channel and equilibrium statistical mechanics principle were used to test the hypothesis of empirically calculating the overall voltage sensitivity of an ion channel on the basis of its closed and open conformations, and determine the contribution of individual residues to the voltage sensing. We examined the theoretical paradigm by performing experimental measurements with Kv1.2 channel and a series of mutants. The correlation between the calculated values and the experimental values is at respective level, R 2 = 0.73. Our report therefore provides in silico prediction of key conformations and has identified additional residues critical for voltage sensing.

AB - Voltage sensing confers conversion of a change in membrane potential to signaling activities underlying the physiological processes. For an ion channel, voltage sensitivity is usually experimentally measured by fitting electrophysiological data to Boltzmann distributions. In our study, a two-state model of the ion channel and equilibrium statistical mechanics principle were used to test the hypothesis of empirically calculating the overall voltage sensitivity of an ion channel on the basis of its closed and open conformations, and determine the contribution of individual residues to the voltage sensing. We examined the theoretical paradigm by performing experimental measurements with Kv1.2 channel and a series of mutants. The correlation between the calculated values and the experimental values is at respective level, R 2 = 0.73. Our report therefore provides in silico prediction of key conformations and has identified additional residues critical for voltage sensing.

UR - http://www.scopus.com/inward/record.url?scp=84859884324&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84859884324&partnerID=8YFLogxK

U2 - 10.1016/j.bpj.2012.03.032

DO - 10.1016/j.bpj.2012.03.032

M3 - Article

C2 - 22768937

AN - SCOPUS:84859884324

VL - 102

SP - 1815

EP - 1825

JO - Biophysical Journal

JF - Biophysical Journal

SN - 0006-3495

IS - 8

ER -