A voltage-sensor water pore.

A voltage-sensor water pore. Research Abstract Details 

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A voltage-sensor water pore. Abstract Text:

J Alfredo Freites,Douglas J Tobias,Stephen H White,

Voltage-sensor (VS) domains cause the pore of voltage-gated ion channels to open and close in response to changes in transmembrane potential. Recent experimental studies suggest that VS domains are independent structural units. This independence is revealed dramatically by a voltage-dependent proton-selective channel (Hv), which has a sequence homologous to the VS domains of voltage-gated potassium channels (Kv). Here we show by means of molecular dynamics simulations that the isolated open-state VS domain of the KvAP channel in a lipid membrane has a configuration consistent with a water channel, which we propose as a common feature underlying the conductance of protons, and perhaps other cations, through VS domains.

A voltage-sensor water pore. Publishing Authors By Initials

JA Freites,DJ Tobias,SH White,

For similar water research abstracts see: water research

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A voltage-sensor water pore. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Biophysical journal

VOLUME: 91

Page Numbers: L90-2

Journal Abbreviation: Biophys. J.

ISSN: 0006-3495

DAY: 29

MONTH: 09

YEAR: 2006

A voltage-sensor water pore. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 370626

A voltage-sensor water pore. Keywords Mesh Terms:

KEYWORDS: Water

MESH TERMS: chemistry

Chemical & Substance for Abstract: A voltage-sensor water pore. Information

Substance Name: Water

Registry Number: 7732-18-5

Grant and Affiliation Information for A voltage-sensor water pore.

AFFILIATION: Institute for Genomics and Bioinformatics, University of California, Irvine, CA 92697, USA.

Country: United States

AGENCY: United States NCRR

GRANT: RR-14812

ACRONYM: RR

MEDLINETA: Biophys J

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