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Bacteriorhodopsin
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
| - | Br is composed of 6 α-helical elements each containing a retinal molecule. The retinal changes its ground state conformation upon binding of a proton, causing the Br to change conformation to the activated state and pump the proton. <scene name='46/463242/Cv/5'>The retinal interacts with hydrophobic and aromatic residues</scene> <ref>PMID:19603754</ref> ({{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}}). | + | Br is composed of 6 α-helical elements each containing a retinal molecule. The retinal changes its ground state conformation upon binding of a proton, causing the Br to change conformation to the activated state and pump the proton. <scene name='46/463242/Cv/5'>The retinal interacts predominantly with hydrophobic and aromatic residues</scene> <ref>PMID:19603754</ref> ({{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}}). |
</StructureSection> | </StructureSection> | ||
== 3D Structures of bacteriorhodopsin == | == 3D Structures of bacteriorhodopsin == | ||
Revision as of 12:05, 30 November 2015
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3D Structures of bacteriorhodopsin
Updated on 30-November-2015
See Also
References
- ↑ Joh NH, Oberai A, Yang D, Whitelegge JP, Bowie JU. Similar energetic contributions of packing in the core of membrane and water-soluble proteins. J Am Chem Soc. 2009 Aug 12;131(31):10846-7. PMID:19603754 doi:10.1021/ja904711k
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