Sandbox Reserved 1757

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== Structural highlights ==
== Structural highlights ==
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The protein is a dimer that contains <scene name='93/934001/Secondary_structure/1'>14 helices and 15 beta sheets</scene> per linked molecule. The ARG 148 forms hydrogen bonds that allow it to pair with Oleic Acid, the protein’s ligand. Protein also requires H2O to be present in order to bind its <scene name='93/934001/Ligand/1'>ligand</scene>. I found it really interesting that the protein only actually attaches to the ligand via small interaction between ARG 148 and water molecules.
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The protein is a dimer that contains <scene name='93/934001/Secondary_structure/1'>14 helices and 15 beta sheets</scene> per linked molecule. The ARG 148 forms hydrogen bonds that allow it to pair with Oleic Acid, the protein’s ligand. Protein also requires H2O to be present in order to bind its <scene name='93/934001/Ligand/2'>ligand</scene>. I found it really interesting that the protein only actually attaches to the ligand via small interaction between ARG 148 and water molecules.

Revision as of 04:21, 13 December 2022

This Sandbox is Reserved from November 4, 2022 through January 1, 2023 for use in the course CHEM 351 Biochemistry taught by Bonnie Hall at the Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1755 through Sandbox Reserved 1764.
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Structural Information on Mevalonate 3,5-bisphosphate decarboxylase

Caption for this structure

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References

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