Sandbox Reserved 802
From Proteopedia
| Line 10: | Line 10: | ||
The <scene name='56/563214/A3_hydrophobic/1'>hydrophobic residues</scene> are observed in grey. These residues are mostly observed in the interior of the enzyme (possibly on the beta sheets). Thus, they are hidden from the aqueous solvent. The <scene name='56/563214/A3_hydrophilic/1'>hydrophilic residues</scene> are observed in red. Notice that the majority of the hydrophilic amino acids are located on the alpha helices that are on the outside of this enzyme. Thus, these residues must interact with the solvent, which is aqueous. Plus, notice that there are about equal amounts of hydrophobic and hydrophilic residues. | The <scene name='56/563214/A3_hydrophobic/1'>hydrophobic residues</scene> are observed in grey. These residues are mostly observed in the interior of the enzyme (possibly on the beta sheets). Thus, they are hidden from the aqueous solvent. The <scene name='56/563214/A3_hydrophilic/1'>hydrophilic residues</scene> are observed in red. Notice that the majority of the hydrophilic amino acids are located on the alpha helices that are on the outside of this enzyme. Thus, these residues must interact with the solvent, which is aqueous. Plus, notice that there are about equal amounts of hydrophobic and hydrophilic residues. | ||
==Solvent== | ==Solvent== | ||
| + | The <scene name='56/563214/A2_water_space_fill/1'>water molecules</scene> that surround the enzyme are observed in blue. The water appears only on the outside of the enzyme. Thus, the interior must contain hydrophobic residues, and water excludes these from solvation (because when water interacts with hydrophobic residues, there is a decrease in entropy - thus, water tries to minimize contact with these amino acids). The exterior of the protein must contain hydrophilic residues that will interact with the water molecules, as all of the blue water molecules surround the exterior of the enzyme. | ||
==The Ligands== | ==The Ligands== | ||
==Ligand Contacts== | ==Ligand Contacts== | ||
==Catalytic Residues== | ==Catalytic Residues== | ||
Revision as of 18:42, 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. |
To get started:
More help: Help:Editing |
|
Contents |
Introduction and General Structure
can be observed. Aldolase is an enzyme that is active during glycolysis, which is an overall series of reactions that produces cellular energy (ATP). Specifically, aldolase catalyzes an aldol cleavage reaction that hydrolyzes fructose 1,6-bisphosphate. It is a tetrameter (four subunits)composed of alpha helices and beta sheets (). Please note that alpha helices are observed in blue, and beta sheets are in yellow. The majority of the helices are located on the surface (outside) of the enzyme, where as most of the sheets are found in the interior. Most likely, polar amino acids are located on the peripheral helices, while hydrophobic or paired-polar amino acids are found within the beta sheet.
Hydrogen and Disulfide Bonds
The for aldolase allow the protein proper stability. Hydrogen bonds are in red (there are plenty of them), and disfulfide bonds would appear as black. However, please note that there are no observable disulfide bonds in this picture. Also, after observing the hydrogen bonds, the beta sheets can be identified as parallel because the hydrogen bonds appear as slanted (or strained) between sheets.
Hydrophobic and Hydrophilic Residues
The are observed in grey. These residues are mostly observed in the interior of the enzyme (possibly on the beta sheets). Thus, they are hidden from the aqueous solvent. The are observed in red. Notice that the majority of the hydrophilic amino acids are located on the alpha helices that are on the outside of this enzyme. Thus, these residues must interact with the solvent, which is aqueous. Plus, notice that there are about equal amounts of hydrophobic and hydrophilic residues.
Solvent
The that surround the enzyme are observed in blue. The water appears only on the outside of the enzyme. Thus, the interior must contain hydrophobic residues, and water excludes these from solvation (because when water interacts with hydrophobic residues, there is a decrease in entropy - thus, water tries to minimize contact with these amino acids). The exterior of the protein must contain hydrophilic residues that will interact with the water molecules, as all of the blue water molecules surround the exterior of the enzyme.
