Sandbox Reserved 819: Difference between revisions

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56% of the Archaeorhodopsin-2 sequence is identical to the Bacteriorhodopsin sequence.<ref name="seq">PMID: 1654776</ref>

56% of the Archaeorhodopsin-2 sequence is identical to the [[Bacteriorhodopsin]] sequence.<ref name="seq">PMID: 1654776</ref>

Most amino acids that play a role in the trimerization are not conserved between the two proteins. For instance, the counterparts of some hydrophobic residues of the Archaerhodopsin-2 (the one interacting with the polyene chain of the bacterioruberin) have a different volume. Another difference is the fact that the hydrophobic residues of the Archaerhodopsin-2 (responsible for the hydrogen bonds with the bacterioruberin) are replaced in the Bacteriorhodopsin by hydrophobic amino acids.

Most amino acids that play a role in the trimerization are not conserved between the two proteins. For instance, the counterparts of some hydrophobic residues of the Archaerhodopsin-2 (the one interacting with the polyene chain of the bacterioruberin) have a different volume. Another difference is the fact that the hydrophobic residues of the Archaerhodopsin-2 (responsible for the hydrogen bonds with the bacterioruberin) are replaced in the [[Bacteriorhodopsin]] by hydrophobic amino acids.

However the global structures of Archaeorhodopsin-2 and Bacteriorhodopsin are really similar, especially at the level of the open space between the monomers. This similarity of structure forms the basis of several hypothesis concerning the mechanisms of the Archaeorhodopsin-2 <ref name="multiple">PMID:18082767</ref>

However the global structures of Archaeorhodopsin-2 and [[Bacteriorhodopsin]] are really similar, especially at the level of the open space between the monomers. This similarity of structure forms the basis of several hypothesis concerning the mechanisms of the Archaeorhodopsin-2 <ref name="multiple">PMID:18082767</ref>

Sandbox Reserved 819: Difference between revisions

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@@ Line 86: / Line 86: @@
-% of the Archaeorhodopsin-2 sequence is identical to the Bacteriorhodopsin sequence.<ref name="seq">PMID: 1654776</ref>
+% of the Archaeorhodopsin-2 sequence is identical to the [[Bacteriorhodopsin]] sequence.<ref name="seq">PMID: 1654776</ref>
-Most amino acids that play a role in the trimerization are not conserved between the two proteins. For instance, the counterparts of some hydrophobic residues of the Archaerhodopsin-2 (the one interacting with the polyene chain of the bacterioruberin) have a different volume. Another difference is the fact that the hydrophobic residues of the Archaerhodopsin-2 (responsible for the hydrogen bonds with the bacterioruberin) are replaced in the Bacteriorhodopsin by hydrophobic amino acids.
+Most amino acids that play a role in the trimerization are not conserved between the two proteins. For instance, the counterparts of some hydrophobic residues of the Archaerhodopsin-2 (the one interacting with the polyene chain of the bacterioruberin) have a different volume. Another difference is the fact that the hydrophobic residues of the Archaerhodopsin-2 (responsible for the hydrogen bonds with the bacterioruberin) are replaced in the [[Bacteriorhodopsin]] by hydrophobic amino acids.
-However the global structures of Archaeorhodopsin-2 and Bacteriorhodopsin are really similar, especially at the level of the open space between the monomers. This similarity of structure forms the basis of several hypothesis concerning the mechanisms of the Archaeorhodopsin-2 <ref name="multiple">PMID:18082767</ref>
+However the global structures of Archaeorhodopsin-2 and [[Bacteriorhodopsin]] are really similar, especially at the level of the open space between the monomers. This similarity of structure forms the basis of several hypothesis concerning the mechanisms of the Archaeorhodopsin-2 <ref name="multiple">PMID:18082767</ref>