Sandbox Reserved 1635

From Proteopedia

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Important amino acids within this protein are asparagine, histidine, and cysteine. Most of the amino acids are bound together by hydrogen bonds. Amino acids form the catalytic residues that lower activation energy in an enzyme-catalyzed reaction.
Important amino acids within this protein are asparagine, histidine, and cysteine. Most of the amino acids are bound together by hydrogen bonds. Amino acids form the catalytic residues that lower activation energy in an enzyme-catalyzed reaction.
== Structural highlights ==
== Structural highlights ==
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In the secondary structure, there are 10 alpha helices <scene name='86/861617/Secondary_structure/2'>Text To Be Displayed</scene>. The tertiary structure contains Citric Acid (CIT) and Sulfate Ion (SO4). There are many Hydrophobic Parts with this protein. <scene name='86/861617/Hydrophobic_parts/1'>Hydrophobic Parts</scene>. Most of the protein is hydrophobic which is all the purple parts.
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In the secondary structure, there are 10 alpha helices <scene name='86/861617/Secondary_structure/2'>Secondary Structure</scene>. The tertiary structure contains Citric Acid (CIT) and Sulfate Ion (SO4). There are many Hydrophobic Parts with this protein. <scene name='86/861617/Hydrophobic_parts/1'>Hydrophobic Parts</scene>. Most of the protein is hydrophobic which is all the purple parts.
== Other important features ==
== Other important features ==
There are two main autocatalytic cleavage sites, Asn333 and Asn345. Upon incubation at pH ,5.0, you can observe additional cleavage sites on the LSAM domain, including Asp363, Asp416, and Asp417. This is important because it initiates Proteolytic Activation. Meaning it's breaking down the proteins into smaller polypeptides or amino acids.
There are two main autocatalytic cleavage sites, Asn333 and Asn345. Upon incubation at pH ,5.0, you can observe additional cleavage sites on the LSAM domain, including Asp363, Asp416, and Asp417. This is important because it initiates Proteolytic Activation. Meaning it's breaking down the proteins into smaller polypeptides or amino acids.

Revision as of 04:49, 8 December 2020

This Sandbox is Reserved from 09/18/2020 through 03/20/2021 for use in CHEM 351 Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, IA. This reservation includes Sandbox Reserved 1628 through Sandbox Reserved 1642.
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Structure

Caption for this structure

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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

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