Sandbox Reserved 1680

From Proteopedia

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== Function of your protein ==
== Function of your protein ==
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a.
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The protein Spy can facilitate protein folding by allowing it to prevent clustering by grabbing the proteins as they start to misfold right before they are able to stick to other proteins to make big cluster. The protein needs to bind very quickly.
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b. Spy's job is to grab proteins as they start to misfold before they can stick to other proteins.
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== Biological relevance and broader implications ==
== Biological relevance and broader implications ==
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<scene name='87/873242/Protein_spy/1'>Protein Spy</scene>
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There are diseases out there wondering if we can customize chaperons. One in particular is Alzheimer's because people with this disease could possibly have differences in their chaperons which could cause you to be more prone to that disease. You can be more prone because of the beta amyloid plaques being formed. By studying this protein and doing different experiments with it was helping to better understand how chaperons work.
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<scene name='87/873242/Protein_spy1/2'>Protein Spy1</scene>
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== Important amino acids==
== Important amino acids==
== Structural highlights ==
== Structural highlights ==
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<scene name='87/873242/Protein_spy/1'>Protein Spy</scene>
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<scene name='87/873242/Protein_spy1/2'>Protein Spy1</scene>
== Other important features ==
== Other important features ==

Revision as of 04:47, 19 April 2021

This Sandbox is Reserved from 01/25/2021 through 04/30/2021 for use in Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1665 through Sandbox Reserved 1682.
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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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