User:Eric Martz/Sandbox 10: Difference between revisions

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</li>
<li>Show <scene name='User:Eric_Martz/Sandbox_10/Hydrated_bilayer_w_gramicidin/1'>water</scene>. Notice how the hydrophobic lipid &quot;tails&quot; exclude water.
<li>Show <scene name='User:Eric_Martz/Sandbox_10/Hydrated_bilayer_w_gramicidin/1'>water</scene>. Notice how the hydrophobic lipid &quot;tails&quot; exclude water.
</li>
<li>Water passes
<scene name='User:Eric_Martz/Sandbox_10/Hydrated_bilayer_w_gramicidin/2'>through the channel</scene>.
</li>
</li>
</ul>
</ul>

Revision as of 04:38, 5 March 2010

Proposed Title: Gramicidin Channel in Lipid Bilayer

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).

Drag the structure with the mouse to rotate

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).

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

ReferencesReferences

  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
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