Sandbox Reserved 819: Difference between revisions

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[[Image:2z55_bio_r_500.jpg|300px|left|thumb|The trimeric structure with its ligands]]

Archaerhodopsin-2 is a retinal protein–carotenoid complex found in the claret membrane of Halorubrum sp. aus-2 and it represents a real adaptation to life at high salt concentrations. In these membranes, three Archaerhodopsin-2 chains form a trimeric structure [http://www.pdb.org/pdb/explore/jmol.do?structureId=2Z55&view=symmetry&bionumber=1], capturing light energy and using it to move protons across the membrane out of the cell. It exists four different chains with different structures: A,B,D,E (they are not represented here).

Archaerhodopsin-2 is a retinal protein–carotenoid complex found in the claret membrane of Halorubrum sp. aus-2 and it represents a real adaptation to life at high salt concentrations. In these membranes, three Archaerhodopsin-2 chains form a trimeric structure [http://www.pdb.org/pdb/explore/jmol.do?structureId=2Z55&view=symmetry&bionumber=1] (the image on the left side represents the trimeric structure), capturing light energy and using it to move protons across the membrane out of the cell. It exists four different chains with different structures: A,B,D,E (they are not represented here).

The trimerization increases the thermal stability of the protein aR2 in the claret membrane of Halorubrum sp. aus-2 and enlarges the pH range where the protein can keep its neutral conformation. Thus, a larger pH gradient can be generated across the membrane, leading to an increased efficiency of the proton pumping. Therefore the trimeric structure is more efficient than the monomeric structure.

Sandbox Reserved 819: Difference between revisions

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@@ Line 19: / Line 19: @@
 [[Image:2z55_bio_r_500.jpg|300px|left|thumb|The trimeric structure with its ligands]]
-Archaerhodopsin-2 is a retinal protein–carotenoid complex found in the claret membrane of Halorubrum sp. aus-2 and it represents a real adaptation to life at high salt concentrations. In these membranes, three Archaerhodopsin-2 chains form a trimeric structure [http://www.pdb.org/pdb/explore/jmol.do?structureId=2Z55&view=symmetry&bionumber=1], capturing light energy and using it to move protons across the membrane out of the cell. It exists four different chains with different structures: A,B,D,E (they are not represented here).
+Archaerhodopsin-2 is a retinal protein–carotenoid complex found in the claret membrane of Halorubrum sp. aus-2 and it represents a real adaptation to life at high salt concentrations. In these membranes, three Archaerhodopsin-2 chains form a trimeric structure [http://www.pdb.org/pdb/explore/jmol.do?structureId=2Z55&view=symmetry&bionumber=1] (the image on the left side represents the trimeric structure), capturing light energy and using it to move protons across the membrane out of the cell. It exists four different chains with different structures: A,B,D,E (they are not represented here).
 The trimerization increases the thermal stability of the protein aR2 in the claret membrane of Halorubrum sp. aus-2 and enlarges the pH range where the protein can keep its neutral conformation. Thus, a larger pH gradient can be generated across the membrane, leading to an increased efficiency of the proton pumping. Therefore the trimeric structure is more efficient than the monomeric structure.