Sandbox Reserved 1061: Difference between revisions

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Another highly conserved residue is the WSGFRP sequence. This nonpolar sequence is found on the surface of the molecule and is exposed to solvent. [[Image:Hydrophobic region pic.png|thumb| Hydrophobic region WSGFRP on the surface of MtNrdH (red) bound to ligand (green).]]For this reason, it has been hypothesized that this sequence plays a role in the binding of thioredoxin reductase.

Arg-68 is responsible for the stabilization of the hydrophobic region of NrdH. Arg-68 has two distinct conformations. In the <scene name='69/694227/Arg_68_conformation_1/3'>first conformation</scene>, Arg-68 is hydrogen bonded to His- 60 and Asp-59. When Arg-68 shifts to its second conformation, it breaks it hydrogen bond with Asp-59. This reduction in hydrogen bonding gives the hydrophobic region more flexibility and is thought to occur when NrdH is in its inactive state.

Arg-68 is responsible for the stabilization of the hydrophobic region of NrdH. Arg-68 has two distinct conformations. In the <scene name='69/694227/Arg_68_conformation_1/3'>first conformation</scene>, Arg-68 is hydrogen bonded to His- 60 and Asp-59. When Arg-68 shifts to its <scene name='69/694227/Arg_68_conformation_2/2'>second conformation</scene>

, it breaks it hydrogen bond with Asp-59. This reduction in hydrogen bonding gives the hydrophobic region more flexibility and is thought to occur when NrdH is in its inactive state.

== Function ==

Sandbox Reserved 1061: Difference between revisions

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@@ Line 21: / Line 21: @@
 Another highly conserved residue is the WSGFRP sequence. This nonpolar sequence is found on the surface of the molecule and is exposed to solvent. [[Image:Hydrophobic region pic.png|thumb| Hydrophobic region WSGFRP on the surface of MtNrdH (red) bound to ligand (green).]]For this reason, it has been hypothesized that this sequence plays a role in the binding of thioredoxin reductase.
-Arg-68 is responsible for the stabilization of the hydrophobic region of NrdH. Arg-68 has two distinct conformations. In the <scene name='69/694227/Arg_68_conformation_1/3'>first conformation</scene>, Arg-68 is hydrogen bonded to His- 60 and Asp-59. When Arg-68 shifts to its second conformation, it breaks it hydrogen bond with Asp-59. This reduction in hydrogen bonding gives the hydrophobic region more flexibility and is thought to occur when NrdH is in its inactive state.
+Arg-68 is responsible for the stabilization of the hydrophobic region of NrdH. Arg-68 has two distinct conformations. In the <scene name='69/694227/Arg_68_conformation_1/3'>first conformation</scene>, Arg-68 is hydrogen bonded to His- 60 and Asp-59. When Arg-68 shifts to its <scene name='69/694227/Arg_68_conformation_2/2'>second conformation</scene>
+, it breaks it hydrogen bond with Asp-59. This reduction in hydrogen bonding gives the hydrophobic region more flexibility and is thought to occur when NrdH is in its inactive state.
 == Function ==