Sandbox Reserved 1692

From Proteopedia

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== Important amino acids==
== Important amino acids==
Amino Acids <scene name='89/892735/Highlighting_amino_acids/2'>85, 150, 166, 170, 202, 220, 275, and 331</scene> provide important interactions for binding. The His105 side chain forms a hydrogen bond with His85 side chain, providing stabilizing assistance. <ref>PMID:34303708</ref>.
Amino Acids <scene name='89/892735/Highlighting_amino_acids/2'>85, 150, 166, 170, 202, 220, 275, and 331</scene> provide important interactions for binding. The His105 side chain forms a hydrogen bond with His85 side chain, providing stabilizing assistance. <ref>PMID:34303708</ref>.
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Amino Acid Residues <scene name='89/892735/Tyr150_and_his85/1'>Tyr150 and His85</scene> form a hydrogen bond with the O-1 atom of Rha, suggesting these residues aid in the stabilization and elimination reactions.
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Amino Acid Residues <scene name='89/892735/Tyr150_and_his85/1'>Tyr150 and His85</scene> form a hydrogen bond with the O-1 atom of Rha, suggesting these residues play a catalytic role for the elimination reaction.
== Structural highlights ==
== Structural highlights ==
Secondary Structure: In this protein, there are around 30 anti-parallel beta sheets, two small hydrophobic alpha helices, and one alpha helix. The anti-parallel beta sheets provide further stabilization, through strong hydrogen bonding in the backbone, of the protein compared to parallel beta sheets. The hydrophobic alpha helices provide structure for the formation of the active site.
Secondary Structure: In this protein, there are around 30 anti-parallel beta sheets, two small hydrophobic alpha helices, and one alpha helix. The anti-parallel beta sheets provide further stabilization, through strong hydrogen bonding in the backbone, of the protein compared to parallel beta sheets. The hydrophobic alpha helices provide structure for the formation of the active site.

Revision as of 14:49, 7 December 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.
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Structure and Function of FoRham1

Structure of FoRham1

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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
  3. Kondo T, Kichijo M, Maruta A, Nakaya M, Takenaka S, Arakawa T, Fushinobu S, Sakamoto T. Structural and functional analysis of gum arabic l-rhamnose-alpha-1,4-d-glucuronate lyase establishes a novel polysaccharide lyase family. J Biol Chem. 2021 Jul 22:101001. doi: 10.1016/j.jbc.2021.101001. PMID:34303708 doi:http://dx.doi.org/10.1016/j.jbc.2021.101001
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