Sandbox 33
From Proteopedia
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<scene name='Sandbox_33/Hydrophilic_better/1'>Hydrophilic easier</scene> | <scene name='Sandbox_33/Hydrophilic_better/1'>Hydrophilic easier</scene> | ||
| - | Perhaps more easily visualized <scene name='Sandbox_33/Hydrophilic_residues_better/1'>here</scene>. | ||
==Solvent== | ==Solvent== | ||
Revision as of 23:54, 19 October 2012
| Please do NOT make changes to this Sandbox. Sandboxes 30-60 are reserved for use by Biochemistry 410 & 412 at Messiah College taught by Dr. Hannah Tims during Fall 2012 and Spring 2013. |
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Contents |
Adenylate Kinase
(also known as 1AKE) is a phosphotransferase enzyme that catalyzes the interconversion of adenine nucleotides. Adenylate Kinase thus plays an important role in cellular metabolism. The images of Adenylate Kinase in this sandbox are from Yersinia Pestis, or yeast.
Secondary Structure
The consists of 214 amino acids which form 12 alpha helices and 7 beta sheets. The helices are displayed in hot pink and the anti-parallel beta sheets are of adenylate kinase are shown in purple. The secondary structure is held together by (depicted by black lines).
Hydrophobic and Hydrophilic Residues
In aqueous, physiological environment the of adenylate kinase, seen in grey, are buried in the interior of the protein. The , seen in yellow, (both polar and charged residues) are on the outside of the protein exposed to the environment. The hydrophobic residues aggregate together (cluster together to avoid the aqueous environment) and bury themselves in the interior of the protein, away from the exterior aqueous environment. Hydrophilic residues are exposed because they can interact with the aqueous environment. Hydrophilic residues can exist on the interior of a protein by interacting with one another and avoiding interaction with hydrophobic residues. Hydrophilic residues can also exist in the active site to stabilize hydrophobic portions of the substrate.
Solvent
write something about where the waters are, and arent
ligand highlighted brown
Enzyme Activity
When you add the green link to the top part of the page, make sure you say something about what kinds of side-chains interact with the non-hydrolysable substrate, and if that makes sense.
catalytic residues, check w/ dr tims to see if i have selected the rite ones
