Gramicidin Channel in Lipid Bilayer
From Proteopedia
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Revision as of 16:17, 28 June 2017
| Theoretical Model: The structure described on this page was determined theoretically (in 1994[1]), and hence should be interpreted with caution. |
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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.
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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
- ↑ 1.0 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
