Bacteriorhodopsin: Difference between revisions
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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/6'>The retinal interacts predominantly 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/6'>The retinal interacts predominantly with hydrophobic and aromatic residues</scene> <ref>PMID:19603754</ref> ({{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}}). | ||
== 3D Structures of bacteriorhodopsin == | |||
[[Bacteriorhodopsin 3D structures]] | |||
</StructureSection> | </StructureSection> | ||
== 3D Structures of bacteriorhodopsin == | == 3D Structures of bacteriorhodopsin == | ||
Revision as of 06:28, 1 April 2019
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3D Structures of bacteriorhodopsin
Updated on 01-April-2019
See Also
References
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Wayne Decatur, Jaime Prilusky, Joel L. Sussman
