Gramicidin Channel in Lipid Bilayer

From Proteopedia

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

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 dioxolane in this experiment (C, O)
• C, H, O, N, P
  (Most hydrogen atoms are omitted.)
• 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.

See Also

• A detailed explanation and tutorial about Lipid Bilayers and the Gramicidin Channel.
• This model in FirstGlance in Jmol. Be sure to click the Ligands+ and Water buttons!
• Lipids: structure and classification
• BioMolecular Explorer 3D, a resource for high school teachers that includes a section on gramicidin in a lipid bilayer.
• High school teachers' resources
• The Spanish version of this page: Canal de gramicidina en bicapa lipídica (Spanish)
• For additional information, see: Membrane Channels & Pumps

Notes

• The PDB file shown here, Image:Gramicidin in bilayer.pdb.gz, was kindly provided by Serge Crouzy^[1].

References

1. ↑ ^{1.0 1.1 1.2} 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