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| - | This sandbox is in use until August 1, 2011 for UMass Chemistry 423. Others please do not edit this page. Thanks!
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| - | Chem423 Team Projects: Understanding Drug Mechanisms
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| - | Andy Kim, Zach Brentzel, Tyler Vlass, Zach Hitzig
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| - | | + | p53 Tumor Supressor gene/HOX gene? |
| - | {{STRUCTURE_1acj | PDB=1acj | SCENE= }}
| + | ===please do not edit this sandbox unless you are part of La Canada High School Protein DNA Institute=== |
| - | | + | == Basic == |
| - | ==Topic: Acetylcholinesterase bound by Tacrine==
| + | ===this is level 3=== |
| - | | + | this is text |
| - | ==Introduction==
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| - | By Tyler Vlass
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| - | ==Overall structure==
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| - | By Zach Brentzel
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| - | {{STRUCTURE_1ea5 | PDB=1ea5 | SCENE= }}
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| - | ¤Acetylcholinesterase (AChE) is a tetramer that is connected to the membrane in neuromuscular junctions by a molecule called collagen Q. [[http://www.ncbi.nlm.nih.gov/pubmed/11804574]]
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| - | ¤Acetylcholinesterase (AChE) is an monomeric enzyme. Most often, AChE forms a tetramer and binds with a molecule, collagen Q, to connect to the membrane of the neuromuscular junction. [[http://www.ncbi.nlm.nih.gov/pubmed/11804574]]. From the <scene name='Sandbox11/Secondary_structure/3'>secondary structure</scene>, it can be seen that there are 17 <scene name='Sandbox11/Alpha_helix_total/4'>alpha helices</scene> and 14 <scene name='Sandbox11/Beta_strands/1'>beta strands</scene>. There are 2 beta sheets formed from 3 anti-parallel and 11 anti-parallel beta sheets, respectively(maybe highlight with green scene). As the <scene name='Sandbox11/Original_structure/3'>overall tertiary structure</scene> shows, turns, alpha helices, and beta sheets all occupy a portion of the exterior of the protein. The means that the turns must be composed primarily of polar side chains. On the other hand, the alpha helices will be amphipathic with side chain order designated by the helical wheel; the exterior will be filled with polar side chains that can hydrogen bond with water while the inside of the alpha helix will have nonpolar, hydrophobic groups. The beta sheets must also be amphipathic, but the pattern of side chains is alternating polar and nonpolar. In addition, in order to maintain its tertiary structure, the protein has two sulfide bonds between CYTOSINE X AND CYTOSINE Y (SHOW DIAGRAM).
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| - | ¤To do: Try to show 4 monomers, better alpha helices, explain polar/nonpolar regions, where binding site is
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| - | <scene name='Sandbox11/Alpha_helix_total/4'>alpha helices</scene>
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| - | <scene name='Sandbox11/Beta_strands/1'>beta strands</scene>
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| - | <scene name='Sandbox11/Original_structure/3'>overall tertiary structure</scene>
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| - | <scene name='Sandbox11/Secondary_structure/3'>secondary structure</scene>
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| - | ==Binding== | + | |
| - | By Andy Kim==
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| - | ==Additional Features== | + | |
| - | By Zach Hitzig
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| - | ==This is a placeholder== | + | |
| - | This is a placeholder text to help you get started in
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| - | placing a Jmol applet on your page. At any time, click
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| - | Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load
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| - | and display another structure.
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| - | Andy Kim, Zach Brentzel, Tyler Vlass, Zach Hitzig-Acetylcholinesterase
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