Sandbox Reserved 798
From Proteopedia
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==Bonding== | ==Bonding== | ||
| - | The <scene name='56/563210/Hydrogen_bonds/2'>hydrogen bonds on the backbone</scene> are colored in orange. Based on the amount of the thin orange lines, it is clear that there are many hydrogen bonds. However, there are no <scene name='56/563210/G-3-p/2'>disulfide bonds</scene> within the structure, or they would have been highlighted in green. The only special binding in the G-3-P enzyme is the hydrogen bonding. Looking at the structure with the <scene name='56/563210/Hydrogen_bonds_and_beta_sheets/1'>beta sheets (dark green) and hydrogen bonding (orange)</scene> highlights the structure of the beta sheets. The image shows that majority of the beta sheets are parallel in structure, but there are a few anti-parallel sections of the beta sheets. | + | The <scene name='56/563210/Hydrogen_bonds/2'>hydrogen bonds on the backbone</scene> are colored in orange. Based on the amount of the thin orange lines, it is clear that there are many hydrogen bonds. However, there are no <scene name='56/563210/G-3-p/2'>disulfide bonds</scene> within the structure, or they would have been highlighted in green. The only special binding in the G-3-P enzyme is the hydrogen bonding. Looking at the structure with the <scene name='56/563210/Hydrogen_bonds_and_beta_sheets/1'>beta sheets (dark green) and hydrogen bonding (orange)</scene> highlights the structure of the beta sheets. When the beta sheets are parallel, the hydrogen bonds are strained at an angle. In the anti-parallel sheets, the bonding is less strained so the hydrogen bonds are perpendicular to beta sheets. The image shows that majority of the beta sheets are parallel in structure, but there are a few anti-parallel sections of the beta sheets. |
==Residues== | ==Residues== | ||
| - | The <scene name='56/563210/Hydrophobic_residues/2'>hydrophobic residues</scene> are shown in grey. The <scene name='56/563210/Hydrophilic_residues/1'>hydrophilic residues</scene> are shown in royal blue. The hydrophobic residues are on the internal part of the enzyme while the hydrophilic sections surround the hydrophobic residues. | + | The <scene name='56/563210/Hydrophobic_residues/2'>hydrophobic residues</scene> are shown in grey. The <scene name='56/563210/Hydrophilic_residues/1'>hydrophilic residues</scene> are shown in royal blue. The hydrophobic residues are on the internal part of the enzyme while the hydrophilic sections surround the hydrophobic residues. The hydrophilic resides on the outside of the enzyme will increase interaction with the surrounding aqueous solvent. |
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==Solvent== | ==Solvent== | ||
| + | |||
==Ligands and Ligand Contacts== | ==Ligands and Ligand Contacts== | ||
| + | ==Catalytic Residues == | ||
==Resources== | ==Resources== | ||
Revision as of 16:08, 15 October 2013
| This Sandbox is Reserved from Oct 10, 2013, through May 20, 2014 for use in the course "CHEM 410 Biochemistry 1 and 2" taught by Hanna Tims at the Messiah College. This reservation includes Sandbox Reserved 780 through Sandbox Reserved 807. |
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Contents |
Glyceraldehyde-3-phosphate dehydrogenase
Introduction and Basic Structure
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Glyceraldehyde-3-phosphate dehydrogenase, or more commonly called, , is a tetrahedral protein. G-3-P is an enzyme used in glycolysis to produce NADH through a mechanism with phosphate and NAD+, which binds to the ligand binding site of G-3-P. The G-3-P is converted to 3-phospho-D-glyceroyl-phosphate. The has both alpha helices (purple) and beta sheets (green). The alpha helices are in four separate sections, but are mostly on the external sections of the enzyme. The beta sheets are closer to the center of the enzyme. The shows a more accurate representation of what this enzyme looks like.
Bonding
The are colored in orange. Based on the amount of the thin orange lines, it is clear that there are many hydrogen bonds. However, there are no within the structure, or they would have been highlighted in green. The only special binding in the G-3-P enzyme is the hydrogen bonding. Looking at the structure with the highlights the structure of the beta sheets. When the beta sheets are parallel, the hydrogen bonds are strained at an angle. In the anti-parallel sheets, the bonding is less strained so the hydrogen bonds are perpendicular to beta sheets. The image shows that majority of the beta sheets are parallel in structure, but there are a few anti-parallel sections of the beta sheets.
Residues
The are shown in grey. The are shown in royal blue. The hydrophobic residues are on the internal part of the enzyme while the hydrophilic sections surround the hydrophobic residues. The hydrophilic resides on the outside of the enzyme will increase interaction with the surrounding aqueous solvent.
