Sandbox Reserved 1679
From Proteopedia
(Difference between revisions)
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{{Sandbox_Reserved_BHall_Sp21}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | {{Sandbox_Reserved_BHall_Sp21}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
==Your Heading Here (maybe something like 'Structure')== | ==Your Heading Here (maybe something like 'Structure')== | ||
- | <StructureSection load=' | + | <StructureSection load='3O39' size='340' side='right' caption='Caption for this structure' scene=''> |
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
- | == Function == | + | == Function of your protein == |
+ | The organism that the chaperone is from is E. Coli | ||
+ | My protein is used to catch miss informed calls and nudge them back into the right shape and to stop them from chunking up, as you can see by the <scene name='87/873241/Second_protein_view/1'>amazing protein</scene> attached. | ||
- | == | + | == Biological relevance and broader implications == |
- | + | A. | |
- | == | + | b. |
+ | c. This study was important to science because it showed what one chaperone can do under different hydrophobic conditions and also what effect the charge had on the protein. It also went into depth about how a good balance is needed between the two. | ||
+ | == Important amino acids== | ||
+ | My protein does not have a ligand present. | ||
+ | Our protein lacks a catalytic triad. | ||
== Structural highlights == | == Structural highlights == | ||
+ | Shown here is the level of hydrophobicity that our protein has, this is very important to the structure because different levels will work better or worse with the different charges<scene name='87/873241/Hydrophobicity/2'>Hydrophobicity</scene> | ||
+ | == Other important features == | ||
+ | Important amino acids, as shown by this <scene name='87/873241/Ligand/1'>amateur drawing</scene>. | ||
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
Current revision
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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Your Heading Here (maybe something like 'Structure')
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References
- ↑ 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
- ↑ 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