The gramicidin a channel

A review of its permeability characteristics with special reference to the single-file aspect of transport

Alan Finkelstein, Olaf Sparre Andersen

Research output: Contribution to journalArticle

239 Citations (Scopus)

Abstract

Gramicidin A forms univalent cation-selective channels of ≈4 Å diameter in phospholipid bilayer membranes. The transport of ions and water throughout most of the channel length is by a singlefile process; that is, cations and water molecules cannot pass each other within the channel. The implications of this single-file mode of transport for ion movement are considered. In particular, we show that there is no significant electrostatic barrier to ion movement between the energy wells at the two ends of the channel. The rate of ion translocation (e.g., Na+ or Cs+) through the channel between these wells is limited by the necessity for an ion to move six water molecules in single file along with it; this also limits the maximum possible value for channel conductance. At all attainable concentrations of NaCl, the gramicidin A channel never contains more than one sodium ion, whereas even at 0.1M CsCl, some channels contain two cesium ions. There is no necessity to postulate more than two ion-binding sites in the channel or occupancy of the channel by more than two ions at any time.

Original languageEnglish (US)
Pages (from-to)155-171
Number of pages17
JournalThe Journal of Membrane Biology
Volume59
Issue number3
DOIs
StatePublished - Oct 1981

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Gramicidin
Permeability
Ions
Ion Transport
Cations
Water
Cesium
Static Electricity
Phospholipids
Sodium
Binding Sites
Membranes

ASJC Scopus subject areas

  • Physiology
  • Cell Biology
  • Biophysics

Cite this

The gramicidin a channel : A review of its permeability characteristics with special reference to the single-file aspect of transport. / Finkelstein, Alan; Andersen, Olaf Sparre.

In: The Journal of Membrane Biology, Vol. 59, No. 3, 10.1981, p. 155-171.

Research output: Contribution to journalArticle

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