Sandbox Reserved 1468
From Proteopedia
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== By studying VesB, improved treatment and prevention of cholera could be discovered. While it is not a major problem in the United States, lives could be improved and saved in areas such such as Africa, where cholera is more prevalent. This would allow more social interaction without concern of disease, which would be beneficial as many people are in close contact in these areas of contamination. == | == By studying VesB, improved treatment and prevention of cholera could be discovered. While it is not a major problem in the United States, lives could be improved and saved in areas such such as Africa, where cholera is more prevalent. This would allow more social interaction without concern of disease, which would be beneficial as many people are in close contact in these areas of contamination. == | ||
- | == The primary <scene name='79/799596/Vesb_secondary_structure/1'>secondary structure</scene> of VesB is beta sheets, with some alpha helices and a few random coils. VesB has two <scene name='79/799596/Disulfide_bonds/1'>disulfide bonds</scene> and <scene name='79/799596/Domains/1'>two domains</scene> that make up its tertiary structure. There is an N-terminal protease domain with a trypsin/chymotrypsin fold and also a C-terminal Ig fold. <scene name='79/799596/Spacefill/1'>VesB space-filling view</scene> shows the size of the protein and the area each molecule occupies. == | + | == The primary <scene name='79/799596/Vesb_secondary_structure/1'>secondary structure</scene> of VesB is beta sheets, with some alpha helices and a few random coils. VesB has two <scene name='79/799596/Disulfide_bonds/1'>disulfide bonds</scene> and <scene name='79/799596/Domains/1'>two domains</scene> that make up its tertiary structure. There is an N-terminal protease domain with a trypsin/chymotrypsin fold and also a C-terminal Ig fold. <scene name='79/799596/Spacefill/1'>VesB space-filling view</scene> shows the size of the protein and the area each molecule occupies. There are both <scene name='79/799596/Hydrophobic_highlighted/1'>hydrophilic and hydrophobic</scene> sections of VesB. Its active site is hydrophobic, as is much of its surface. The alpha helices make up the majority of the hydrophilic areas, showing areas where water would be attracted to VesB. The crystal structure of VesB was solved without a ligand, however, any protein containing RX is a VesB ligand. == |
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 23:20, 16 November 2018
This Sandbox is Reserved from October 22, 2018 through April 30, 2019 for use in the course Biochemistry taught by Bonnie Hall at the Grand View University, Des Moines, IA USA. This reservation includes Sandbox Reserved 1456 through Sandbox Reserved 1470. |
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VesB Structure
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