Sandbox Reserved 1692

From Proteopedia

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== Function of your protein ==
== Function of your protein ==
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Our protein, L-rhamnose- α-1,4-D-glucuronate lyase (FoRham1), derived from the fungus Fusarium oxysporum, is a helpful tool for determining the structure and function of Gum Arabic (GA) to create potential agents to degrade GA more effectively. FoRham1, when bound to GA, will remove the Rha-caps from the nonreducing ends of GA. Understanding the mechanism will give researchers more tools to understand how to degrade GA. Specifically, I focused on the mutant H105F, which has a PDB file of 7ESN.
Here, I have the protein <scene name='89/892735/Protein_view_2/3'>with bound ligand.</scene>
Here, I have the protein <scene name='89/892735/Protein_view_2/3'>with bound ligand.</scene>
== Biological relevance and broader implications ==
== Biological relevance and broader implications ==

Revision as of 03:59, 8 November 2021

This Sandbox is Reserved from 10/01/2021 through 01/01//2022 for use in Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1690 through Sandbox Reserved 1699.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

Structure of FoRham1 (maybe something like 'Structure')

FoRham1

Drag the structure with the mouse to rotate

References

  1. Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
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