The interaction of Cl- with a gramicidin-like channel

Shen Shu Sung; Peter C. Jordan

doi:10.1016/0301-4622(87)80041-8

The interaction of Cl^- with a gramicidin-like channel

Shen Shu Sung, Peter C. Jordan

Department of Pharmacology

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Abstract

Molecular dynamics simulations have been used to study the interaction of Cl^- with a gramicidin-like channel. The results suggest that there is a high-energy barrier at the entrance of the channel, which would correspond to a permeability 10^-9-times that of a cation of the same size. This could account for the cationic selectivity of the gramicidin channel and indicates that valence selectivity is kinetically controlled.

Original language	English (US)
Pages (from-to)	1-6
Number of pages	6
Journal	Biophysical Chemistry
Volume	27
Issue number	1
DOIs	https://doi.org/10.1016/0301-4622(87)80041-8
State	Published - Jul 1987

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Organic Chemistry

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10.1016/0301-4622(87)80041-8

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abstract = "Molecular dynamics simulations have been used to study the interaction of Cl- with a gramicidin-like channel. The results suggest that there is a high-energy barrier at the entrance of the channel, which would correspond to a permeability 10-9-times that of a cation of the same size. This could account for the cationic selectivity of the gramicidin channel and indicates that valence selectivity is kinetically controlled.",

author = "Sung, {Shen Shu} and Jordan, {Peter C.}",

note = "Funding Information: This work has been supported by NIH grant GM-28643.",

year = "1987",

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AB - Molecular dynamics simulations have been used to study the interaction of Cl- with a gramicidin-like channel. The results suggest that there is a high-energy barrier at the entrance of the channel, which would correspond to a permeability 10-9-times that of a cation of the same size. This could account for the cationic selectivity of the gramicidin channel and indicates that valence selectivity is kinetically controlled.

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The interaction of Cl^- with a gramicidin-like channel

Abstract

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