Gramicidin Channel in Lipid Bilayer

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Theoretical Model: The structure described on this page was determined theoretically (in 1994[1]), and hence should be interpreted with caution.

Theoretical model of gramicidin in a lipid bilayer (phosphatidyl ethanolamine).

The scenes on this page have been repaired. Eric Martz 00:37, 30 September 2014 (IST)

Two copies of the 15-amino-acid gramicidin peptide are shown here () arranged as they are believed to be when they form a channel through a lipid bilayer membrane[1]. The shape of the protein is shown with tiny dots, inside of which is a ribbon backbone trace connecting the alpha carbon atoms of each amino acid chain.

  • Show of the gramicidin protein chains. The chains are covalently linked with dioxane in this experiment (C, O),
  • (Most hydrogen atoms are omitted.)
    C, H, O, N, P.
  • Show . Notice how the hydrophobic lipid "tails" exclude water.
  • Water passes .
  • Show .

  • Show only .
    C, H, O, N, P.
    For an explanation of their structure, see the detailed tutorial, also disponible en español.

Remember to use the popup button and then resize the popup window to enlarge the molecular scenes.

See Also

Notes

References

  1. 1.0 1.1 Crouzy S, Woolf TB, Roux B. A molecular dynamics study of gating in dioxolane-linked gramicidin A channels. Biophys J. 1994 Oct;67(4):1370-86. PMID:7529578 doi:http://dx.doi.org/10.1016/S0006-3495(94)80618-6

Proteopedia Page Contributors and Editors (what is this?)

Eric Martz, David Canner, Angel Herraez, Jaime Prilusky

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