Theoretical study of the antiparallel double-stranded helical dimer of gramicidin as an ion channel.
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.
Sung
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Department of Chemistry, Brandeis University, Waltham, Massachusetts 02254.
Jordan
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PC
D006096:Gramicidin; D007473:Ion Channels / Q000502:physiology*; D008564:Membrane Potentials; D008954:Models, Biological; D008958:Models, Molecular; D011487:Protein Conformation
D007473:Ion Channels; D006096:Gramicidin