Sandbox Reserved 1061: Difference between revisions

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Another highly conserved series of residues 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).]]<ref>DOI 10.1002/ijch.201300024</ref> <ref>PMID:21638687</ref> For this reason, it has been hypothesized that this sequence plays a role in the binding of thioredoxin reductase. <ref name="Swastik" />[[Image:Wsgfrpweblogo.png|thumb|center|upright=2.5|Weblogo diagram showing highly conserved WSGFRP region of NrdH in five separate protein structures from ''Nocardiaseriolae'', ''E. coli'', ''Cornebacterium Ammoniagenes'', and ''Mycobacterium Tuberculosis''.]]

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>

<scene name='69/694227/Arg_68/4'>Arg-68</scene> 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_1/4'>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_2/5'>second conformation</scene>, it breaks its hydrogen bond with Asp-59. <ref name="Swastik" /> This reduction in hydrogen bonding gives the hydrophobic region more flexibility and is thought to occur when NrdH is in its inactive state.

, it breaks its hydrogen bond with Asp-59. <ref name="Swastik" /> This reduction in hydrogen bonding gives the hydrophobic region more flexibility and is thought to occur when NrdH is in its inactive state.

==== Stabilization ====

Sandbox Reserved 1061: Difference between revisions

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 Another highly conserved series of residues 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).]]<ref>DOI 10.1002/ijch.201300024</ref> <ref>PMID:21638687</ref> For this reason, it has been hypothesized that this sequence plays a role in the binding of thioredoxin reductase. <ref name="Swastik" />[[Image:Wsgfrpweblogo.png|thumb|center|upright=2.5|Weblogo diagram showing highly conserved WSGFRP region of NrdH in five separate protein structures from ''Nocardiaseriolae'', ''E. coli'', ''Cornebacterium Ammoniagenes'', and ''Mycobacterium Tuberculosis''.]]
-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>
+<scene name='69/694227/Arg_68/4'>Arg-68</scene> 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_1/4'>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_2/5'>second conformation</scene>, it breaks its hydrogen bond with Asp-59. <ref name="Swastik" /> This reduction in hydrogen bonding gives the hydrophobic region more flexibility and is thought to occur when NrdH is in its inactive state.
-, it breaks its hydrogen bond with Asp-59. <ref name="Swastik" /> This reduction in hydrogen bonding gives the hydrophobic region more flexibility and is thought to occur when NrdH is in its inactive state.
 ==== Stabilization ====