Sandbox Reserved 796
From Proteopedia
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== Hydrophobic and Hydrophilic Residues == | == Hydrophobic and Hydrophilic Residues == | ||
The <scene name='56/563208/Hydrophobic/2'>hydrophobic residues</scene> are in orange while the <scene name='56/563208/Hydrophilic/1'>hydrophilic residues</scene> are in teal. | The <scene name='56/563208/Hydrophobic/2'>hydrophobic residues</scene> are in orange while the <scene name='56/563208/Hydrophilic/1'>hydrophilic residues</scene> are in teal. | ||
| - | Based on this model, we can conclude that the enzyme is | + | Based on this model, we can conclude that the enzyme is made out of a roughly equal amount of both hydrophobic and hydrophilic residues. |
| - | + | ||
== Solvent == | == Solvent == | ||
Revision as of 18:36, 12 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 |
Introduction and General Structure
is an enzyme in glycolysis. Fructose-1,6-bisphosphate aldolase is a tetramer, has alpha helices in pinkish purple and beta sheets in blue. The alpha helices are mostly found on the surface of the enzyme while the beta sheets are embedded in the inside of the enzyme.
Hydrogen and Disulfide Bond
are in black and there is no observable disulfide bond in the enzyme. Based on the position of the Hydrogen bonds, we concluded that the beta sheets are parallel to each other since the H-bonds are slanted.
Hydrophobic and Hydrophilic Residues
The are in orange while the are in teal. Based on this model, we can conclude that the enzyme is made out of a roughly equal amount of both hydrophobic and hydrophilic residues.
