Sandbox Reserved 796

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== Hydrogen and Disulfide Bond ==
== Hydrogen and Disulfide Bond ==
<scene name='56/563208/H-bond_and_disulfide_bond/1'>Hydrogen bonds</scene> are in black and there is no observable disulfide bond in the enzyme.
<scene name='56/563208/H-bond_and_disulfide_bond/1'>Hydrogen bonds</scene> are in black and there is no observable disulfide bond in the enzyme.
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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.
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== Hydrophobic and Hydrophilic Residues ==
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<scene name='56/563208/Hydrophobic/1'>Hydrophobic residues</scene> are in light purple color.
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<scene name='56/563208/Hydrophobic_and_hydrophillic/1'>Hydrophilic residues</scene> are in teal.

Revision as of 18:23, 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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Fructose-1,6-bisphosphate aldolase

Drag the structure with the mouse to rotate

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

are in light purple color. are in teal.

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