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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/3'>The retinal interacts with hydrophobic and aromatic residues</scene>. | + | 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/3'>The retinal interacts with hydrophobic and aromatic residues</scene>.{{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}} |
</StructureSection> | </StructureSection> | ||
== 3D Structures of bacteriorhodopsin == | == 3D Structures of bacteriorhodopsin == | ||
Revision as of 11:56, 30 November 2015
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3D Structures of bacteriorhodopsin
Updated on 30-November-2015
See Also
References
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Joel L. Sussman, Wayne Decatur, Jaime Prilusky
