We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

Sandbox Reserved 803

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 9: Line 9:
<scene name='56/563215/Color_coded_helices_and_sheets/1'>Hexokinase</scene>, also known as <scene name='56/563215/Color_coded_helices_and_sheets/1'>glucokinase</scene>, is an enzyme that facilitates the phosphorylation of glucose to glucose-6-phosphate in the first step of glycolysis. Glycolysis is the process by which cells break down a molecule of glucose to release energy which can then be used for various cellular processes. In the image to the right, the helices are shown in a brown, while the sheets are a green color. The other colored space filling model in the image is a glucose molecule, which is the ligand in this enzyme catalyzed reaction.
<scene name='56/563215/Color_coded_helices_and_sheets/1'>Hexokinase</scene>, also known as <scene name='56/563215/Color_coded_helices_and_sheets/1'>glucokinase</scene>, is an enzyme that facilitates the phosphorylation of glucose to glucose-6-phosphate in the first step of glycolysis. Glycolysis is the process by which cells break down a molecule of glucose to release energy which can then be used for various cellular processes. In the image to the right, the helices are shown in a brown, while the sheets are a green color. The other colored space filling model in the image is a glucose molecule, which is the ligand in this enzyme catalyzed reaction.
-
Glucokinase has many <scene name='56/563215/Hydrogen_bonds/1'>hydrogen bonds</scene> which are used to hold different parts of the protein together. (unfortunately, the link often doesn't work so I am unable to describe how they affect the protein structure specifically.) Hydrogen bonding in the beta sheets can determine if the sheets are parallel or antiparallel. A parallel sheet will have hydrogen bonds that are not formed at right angles to the sheet, while in an antiparallel sheet, the bonds will be about perpendicular to the sheets.
+
Hexokinase has many <scene name='56/563215/Hydrogen_bonds/1'>hydrogen bonds</scene> which are used to hold different parts of the protein together. (unfortunately, the link often doesn't work so I am unable to describe how they affect the protein structure specifically.) Hydrogen bonding in the beta sheets can determine if the sheets are parallel or antiparallel. A parallel sheet will have hydrogen bonds that are not formed at right angles to the sheet, while in an antiparallel sheet, the bonds will be about perpendicular to the sheets. Disulfide bonds are not seen in hexokinase because the protein is an intercellular protein, and the intercellular environment is reducing, meaning that most disulfide bonds will be reduced inside the cell.
-
<scene name='56/563215/Hydrophobic_residues/2'>Hydrophobic residues</scene>
+
<scene name='56/563215/Hydrophobic_residues/2'>Hydrophobic residues</scene>, colored lime green, are mostly found inside the protein, while the <scene name='56/563215/Hydrophilic_residues/1'>hydrophilic residues</scene> are mostly found on the outside of the protein. This is due to the interaction of the protein with the intercellular <scene name='56/563215/Water_and_ligand/1'>water</scene> molecules, which push hydrophobic residues into the center of the protein by the hydrophobic effect, while making hydrogen bonds with the polar residues on the outside.
<scene name='56/563215/Hydrophobic_hydrophilic/1'>hydrophobic and hydrophilic residues</scene>
<scene name='56/563215/Hydrophobic_hydrophilic/1'>hydrophobic and hydrophilic residues</scene>
-
<scene name='56/563215/Hydrophilic_residues/1'>Hydrophilic residues</scene>
 
-
<scene name='56/563215/Water_and_ligand/1'>water and ligand</scene>
+
 
 +
 
<scene name='56/563215/Interaction_with_substrate/2'>interaction 2</scene>
<scene name='56/563215/Interaction_with_substrate/2'>interaction 2</scene>
<scene name='56/563215/Active_site/1'>active site</scene>
<scene name='56/563215/Active_site/1'>active site</scene>

Revision as of 00:47, 18 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:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

Glucokinase

Drag the structure with the mouse to rotate


Hexokinase (Glucokinase)

, also known as , is an enzyme that facilitates the phosphorylation of glucose to glucose-6-phosphate in the first step of glycolysis. Glycolysis is the process by which cells break down a molecule of glucose to release energy which can then be used for various cellular processes. In the image to the right, the helices are shown in a brown, while the sheets are a green color. The other colored space filling model in the image is a glucose molecule, which is the ligand in this enzyme catalyzed reaction.

Hexokinase has many which are used to hold different parts of the protein together. (unfortunately, the link often doesn't work so I am unable to describe how they affect the protein structure specifically.) Hydrogen bonding in the beta sheets can determine if the sheets are parallel or antiparallel. A parallel sheet will have hydrogen bonds that are not formed at right angles to the sheet, while in an antiparallel sheet, the bonds will be about perpendicular to the sheets. Disulfide bonds are not seen in hexokinase because the protein is an intercellular protein, and the intercellular environment is reducing, meaning that most disulfide bonds will be reduced inside the cell.

, colored lime green, are mostly found inside the protein, while the are mostly found on the outside of the protein. This is due to the interaction of the protein with the intercellular molecules, which push hydrophobic residues into the center of the protein by the hydrophobic effect, while making hydrogen bonds with the polar residues on the outside.



Personal tools