Sandbox Reserved 1569

From Proteopedia

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When looking at a space-fill view of Bap1 and colored based on hydrophobicity, one can easily identify the binding pocket that carbohydrates bind to in the β-prism. Bap1 is known for its sugar binding properties.
When looking at a space-fill view of Bap1 and colored based on hydrophobicity, one can easily identify the binding pocket that carbohydrates bind to in the β-prism. Bap1 is known for its sugar binding properties.
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It is important to note that this protein did not have a catalytic triad mentioned in the paper. Instead, highlighting the key amino acids that are important to the function of Bap1 should be mentioned. These amino acids are Gly 344, Ala 345, Val 346, Lys 501, Asp 348, and His 500.
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It is important to note that this protein did not have a catalytic triad mentioned in the paper. Instead, highlighting the key amino acids that are important to the function of Bap1 should be mentioned. These amino acids are Gly 344, Ala 345, Val 346, Lys 501, Asp 348, and His 500. The actual ligand was not mentioned in the paper either, but citrate was bound near the sites and can be used for important functionality of the protein. Gly 344, Ala 345, Val 346, Lys 501 all interact with citrate via hydrogen bonding. Asp 348 and His 500 interact with citrate via van der Waals interactions.
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== Energy Transformation ==
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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.

Revision as of 02:19, 1 December 2019

This Sandbox is Reserved from Aug 26 through Dec 12, 2019 for use in the course CHEM 351 Biochemistry taught by Bonnie_Hall at the Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1556 through Sandbox Reserved 1575.
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

Bap1

Caption for this structure

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

<https://www.cdc.gov/cholera/general/index.html/> <https://learn-us-east-1-prod-fleet01-xythos.s3.us-east-1.amazonaws.com/5b158bd279e57/1084854?response-content-disposition=inline%3B%20filename%2A%3DUTF-8%27%27J.%2520Biol.%2520Chem.-2019-Kaus-14499-511%2520Bap1%2520and%2520Biofilms.pdf&response-content-type=application%2Fpdf&X-Amz-Algorithm=AWS4-HMAC-SHA256&X-Amz-Date=20191129T222123Z&X-Amz-SignedHeaders=host&X-Amz-Expires=21599&X-Amz-Credential=AKIAIBGJ7RCS23L3LEJQ%2F20191129%2Fus-east-1%2Fs3%2Faws4_request&X-Amz-Signature=ed78695b2e7f71eacab1d648cabfd0bdc32d25d4c7e7baa05f136386ac3844b6/> [1]

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