Sandbox Reserved 1569
From Proteopedia
(Difference between revisions)
| Line 10: | Line 10: | ||
Understanding the structures of what makes up ''Vibrio Cholerae'' would be beneficial to treating the disease. Biofilms are extremely difficult to get rid of. Being able to break up the biofilm naturally and easily lead to less complications and less people dying from losing so much liquid. | Understanding the structures of what makes up ''Vibrio Cholerae'' would be beneficial to treating the disease. Biofilms are extremely difficult to get rid of. Being able to break up the biofilm naturally and easily lead to less complications and less people dying from losing so much liquid. | ||
== Structural highlights and structure-function relationships == | == Structural highlights and structure-function relationships == | ||
| - | There are many key structures one can highlight for Bap1, such as its two different sized connected domains, 8-bladed β-propeller region, active site location outside of the central cavity, and carbohydrate binding site. When looking at the (secondary structure) of Bap1, the two different sized domains are easily seen. The larger domain of the protein is the 8-bladed β-propeller region. The smaller domain of the protein is a β-prism that is connected to the propeller region via a loop in between blade 6. When zooming in on what connects them, it is just two small strands. This makes the protein very flexible. | + | There are many key structures one can highlight for Bap1, such as its two different sized connected domains, 8-bladed β-propeller region, active site location outside of the central cavity, and carbohydrate binding site. |
| + | When looking at the (secondary structure) of Bap1, the two different sized domains are easily seen. The larger domain of the protein is the 8-bladed β-propeller region. The smaller domain of the protein is a β-prism that is connected to the propeller region via a loop in between blade 6. When zooming in on what connects them, it is just two small strands. This makes the protein very flexible. | ||
| + | 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. | ||
== Energy Transformation == | == Energy Transformation == | ||
Revision as of 02:11, 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:
More help: Help:Editing |
Bap1
| |||||||||||
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
<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]
