Sandbox Reserved 796
From Proteopedia
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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. Hydrogen bonding holds the molecule together (especially in secondary structure) and stabilizes the enzyme. |
| - | Based on the position of the | + | 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 between sheets. |
| - | + | ||
== Hydrophobic and Hydrophilic Residues == | == Hydrophobic and Hydrophilic Residues == | ||
Revision as of 13:58, 16 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, the metabolic pathway that converts glucose into pyruvate and produces cellular energy in form of ATP (adenosine triphosphate). Aldolase catalyzes an aldol cleavage reaction that hydrolyzes fructose 1,6-bisphosphate. 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 (outside) 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. Hydrogen bonding holds the molecule together (especially in secondary structure) and stabilizes 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 between sheets.
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.
Solvent
(colored in cream) surrounded the enzyme, which indicated that the residues that made up the surface of the enzyme is hydrophilic. With 50% transparency, no water molecules is observed to be inside the enzyme, which indicated that the inner surface of the enzyme must be hydrophobic.
The ligands and ligand contacts
is in purple. There are three other ligands in the other subunits (B, C, and D).
Catalytic Residues
are Asn33(A)-Glu187(A)-Lys229(A)(in red)
