Theoretical study of the antiparallel double-stranded helical dimer of gramicidin as an ion channel

S. S. Sung, P. C. Jordan

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Recent experimental studies by Durkin, J. T., O. S. Andersen, F. Heitz, Y. Trudelle, and R. E. Koeppe II (1987. Biophys. J. 51:451a) have suggested that the antiparallel double-stranded helical (APDS) dimer of gramicidin can form a transmembrane cation channel. This article reports a theoretical study that successfully rationalizes the channel properties of the APDS dimer. As in the case of the head-to-head (HH) dimer, the APDS exhibits a high potential energy barrier as anions approach the channel mouth, according for the observation of valence selectivity. The calculated potential energies of cations show two binding sites near the channel mouths, a typical feature of the HH channel. The potential energies of hydrated cations in the APDS are generally higher than those in the HH channel and show a larger pseudoperiodicity and higher barriers, an observation which suggests that the APDS should exhibit lower single channel conductance.

Original languageEnglish (US)
Pages (from-to)519-526
Number of pages8
JournalBiophysical journal
Volume54
Issue number3
DOIs
StatePublished - Jan 1 1988

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Gramicidin
Ion Channels
Cations
Theoretical Models
Mouth
Observation
Anions
Binding Sites

All Science Journal Classification (ASJC) codes

  • Biophysics

Cite this

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Theoretical study of the antiparallel double-stranded helical dimer of gramicidin as an ion channel. / Sung, S. S.; Jordan, P. C.

In: Biophysical journal, Vol. 54, No. 3, 01.01.1988, p. 519-526.

Research output: Contribution to journalArticle

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