Sandbox Reserved 819: Difference between revisions

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Archaerhodopsin-2 (aR2) is a light-driven proton pump. It is a retinal protein–carotenoid complex found in the claret membrane of Halorubrum sp. aus-2 and represents a real adaptation to life at high salt concentrations . In these membranes, three Archaerhodopsin-2 or 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). The resulting proton gradient is subsequently converted into chemical energy. 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 purple conformation.~~The trimerization also increases the efficiency of the proton pumping power~~, ~~which is defined by the largest~~ pH gradient ~~that the proton pump~~ can ~~generate~~ across the membrane. ~~So,~~ the trimeric structure is more efficient than the monomeric structure.

Archaerhodopsin-2 (aR2) is a light-driven proton pump. It is a retinal protein–carotenoid complex found in the claret membrane of Halorubrum sp. aus-2 and represents a real adaptation to life at high salt concentrations . In these membranes, three Archaerhodopsin-2 or 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). The resulting proton gradient is subsequently converted into chemical energy. 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 purple 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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Revision as of 16:56, 3 January 2014 view source Lydwine Germain (talk \| contribs) 55 edits No edit summary ← Older edit		Revision as of 17:01, 3 January 2014 view source Lydwine Germain (talk \| contribs) 55 edits No edit summary Newer edit →
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	Archaerhodopsin-2 (aR2) is a light-driven proton pump. It is a retinal protein–carotenoid complex found in the claret membrane of Halorubrum sp. aus-2 and represents a real adaptation to life at high salt concentrations . In these membranes, three Archaerhodopsin-2 or 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). The resulting proton gradient is subsequently converted into chemical energy. 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 purple conformation.~~The trimerization also increases the efficiency of the proton pumping power~~, ~~which is defined by the largest~~ pH gradient ~~that the proton pump~~ can ~~generate~~ across the membrane. ~~So,~~ the trimeric structure is more efficient than the monomeric structure.		Archaerhodopsin-2 (aR2) is a light-driven proton pump. It is a retinal protein–carotenoid complex found in the claret membrane of Halorubrum sp. aus-2 and represents a real adaptation to life at high salt concentrations . In these membranes, three Archaerhodopsin-2 or 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). The resulting proton gradient is subsequently converted into chemical energy. 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 purple 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.