User:Eric Martz/Sandbox 10
From Proteopedia
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| - | Two copies of the gramicidin protein are shown here (<scene name='User:Eric_Martz/Sandbox_10/Gramicidin/4'>restore initial scene</scene>) arranged as they are believed to be when they form a channel through a lipid bilayer membrane. 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). | + | Two copies of the gramicidin protein are shown here (<scene name='User:Eric_Martz/Sandbox_10/Gramicidin/4'>restore initial scene</scene>) arranged as they are believed to be when they form a channel through a lipid bilayer membrane<ref>PMID: 7529578</ref>. 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). |
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Revision as of 01:26, 5 March 2010
Proposed Title: Gramicidin Channel in Lipid Bilayer
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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.)
References
- ↑ 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
