Sandbox Reserved 1061: Difference between revisions
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[[Image:Weblogocvqc.png|thumb|center|upright=2.5|Weblogo diagram showing highly conserved CVQC region of NrdH.]] | [[Image:Weblogocvqc.png|thumb|center|upright=2.5|Weblogo diagram showing highly conserved CVQC region of NrdH.]] | ||
Another highly conserved residue is the WSGFRP sequence. This nonpolar sequence is found on the surface of the molecule and is exposed to solvent. For this reason, it has been hypothesized that this sequence plays a role in the binding of thioredoxin reductase. | 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:Image:Hydrophobic region pic.png|thumb]]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 first conformation, 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 first conformation, 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. | ||
