Gramicidin Channel in Lipid Bilayer

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Theoretical Model: The structure described on this page was determined theoretically, and hence should be interpreted with caution.

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

We apologize, but most of the scenes (green links) on this page are broken. We are working to repair this page. Eric Martz 03:07, 16 August 2014 (IDT)

TEST FOR DEVELOPMENT:

Two copies of the gramicidin protein 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 transparent (ghostly), and a backbone trace connecting the alpha carbon atoms of each amino acid chain is opaque (solid). Toggle spin off to see transparency.

  • Show of the gramicidin protein chains.
  • (Most hydrogen atoms are omitted.)
  • Show . Notice how the hydrophobic lipid "tails" exclude water.
  • Water passes . Toggle spin off to see transparency.
  • Show .

  • Show only . 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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