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		<id>https://proteopedia.org/index.php?title=CBI_Molecules&amp;diff=1332964</id>
		<title>CBI Molecules</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=CBI_Molecules&amp;diff=1332964"/>
		<updated>2011-12-16T20:02:32Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;These are molecules under study by members of the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program].&lt;br /&gt;
Many of the  molecules we study are featured at the [http://www.molecularplayground.org/ Molecular Playground] (see also [[Molecular Playground|Molecular Playground in Proteopedia]]). Follow the links below to read nontechnical descriptions, in Proteopedia, of these molecules.&lt;br /&gt;
&lt;br /&gt;
UMass CBI Members, add your molecules to the list (which is alphabetical by CBI research mentor); follow the instructions below the list.&lt;br /&gt;
&lt;br /&gt;
It&#039;s great to build on a previous entry, but you must leave the earlier one intact and make a copy that you improve and mark as new.  Later we will retain the new one with a merged author list.&lt;br /&gt;
&lt;br /&gt;
Fall 2011: New entries are due 12/16/11. Please append the designation (new Fall 2011) to your new entries. &lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
==Molecules==&lt;br /&gt;
Bhatia Lab&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Alginate-Fall2011]]&#039;&#039;&#039;, Joe White, David Griffin&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Alginate-Fall2010]]&#039;&#039;&#039;, Joe White, David Griffin&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Poly(ethylene glycol)]]&#039;&#039;&#039;, Erika M. Saffer&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[http://chamberslab.com/wp/ Chambers Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Glutamate Receptor]]&#039;&#039;&#039;,  Amanda Hussey, Steve McCarron, Rosie Combs-Bachmann, Mariel Feliciano&lt;br /&gt;
&lt;br /&gt;
[http://openwetware.org/wiki/Chien Chien Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Hexameric ClpX]]&#039;&#039;&#039;, Joanne Lau &lt;br /&gt;
:: Best CBI Molecule 2011&lt;br /&gt;
&lt;br /&gt;
Forbes Lab&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/CheR]]&#039;&#039;&#039;,  Miaomin Zhang&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/RBP]]&#039;&#039;&#039;,  Jan Panteli&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/TRAIL]]&#039;&#039;&#039;,  Charley Swofford&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[http://www.biochem.umass.edu/garman/index.html Garman Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Human Protective Protein Cathepsin A]]&#039;&#039;&#039;, Yadilette Rivera-Colon&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Human PPCA]]&#039;&#039;&#039;, Nilima Kolli&lt;br /&gt;
&lt;br /&gt;
[http://people.chem.umass.edu/gieraschlab/ Gierasch Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[CRABP I ( Cellular Retinoic Acid Binding Protein )|Molecular Playground/CRABP I]]&#039;&#039;&#039;, Kristine Faye Pobre, Mylene Ferrolino,Mangai Periasamy&lt;br /&gt;
:: Best Overall CBI Molecule 2010&lt;br /&gt;
&lt;br /&gt;
: NEW Fall 2011! &#039;&#039;&#039;[[Molecular_Playground/DHFR]]&#039;&#039;&#039;, Karan Hingorani &lt;br /&gt;
&lt;br /&gt;
[http://people.chem.umass.edu/jhardy/ Hardy Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Caspase-7 Dynamics]]&#039;&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Caspase-9 Regulation]]&#039;&#039;&#039;, Kristen Huber&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Caspase-6 (new)]]&#039;&#039;&#039;, Elih Velazquez&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Influenza A M2 transmembrane domain]]&#039;&#039;&#039;, Samantha Nicholls&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Dengue Virus Protease]]&#039;&#039;&#039;, Muslum Yildiz&lt;br /&gt;
&lt;br /&gt;
Hebert Lab&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Saposin C]]&#039;&#039;&#039;, Abla Tannous&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular_Playground/ERMan1]]&#039;&#039;&#039;,  Johan Sunryd&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[http://people.biochem.umass.edu/aheuck/aph.html Heuck Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular_Playground/Pcr H]]&#039;&#039;&#039;,  Fabian Romano&lt;br /&gt;
&lt;br /&gt;
[http://www.chem.umass.edu/people/kaltashovlab/ Kaltashov Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Velaglucerase]]&#039;&#039;&#039;, Adriana Kita &lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Knapp lab&lt;br /&gt;
 &lt;br /&gt;
:&#039;&#039;&#039;[[Molecular Playground/Prolyl Hydroxylase Domain (PHD) Enzyme]]&#039;&#039;&#039;, Cristina Martin&lt;br /&gt;
:: Best CBI Molecule Proteopedia Page 2010&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/FIH]]&#039;&#039;&#039;,  Cornelius Taabazuing, Breanne Holmes, John Hangasky&lt;br /&gt;
&lt;br /&gt;
[http://www.chem.umass.edu/~cmartin/ Martin Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/T7 RNAP Conformations]]&#039;&#039;&#039;, Luis E. Ramirez-Tapia &lt;br /&gt;
:: Best CBI Molecule 2011&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/T7 RNA Polymerase (7 mer int)]]&#039;&#039;&#039;, Ankit Vahia&lt;br /&gt;
&lt;br /&gt;
: NEW Fall 2011! &#039;&#039;&#039;[[Molecular Playground/Human mtRNA pol]]&#039;&#039;&#039;, Ketan Mathavan &lt;br /&gt;
&lt;br /&gt;
[http://roberts.openwetware.org/ Roberts Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Taxol]]&#039;&#039;&#039;,  Rohan Patil, Sarah Wilson&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Insulin]]&#039;&#039;&#039;, Whitney Stoppel&lt;br /&gt;
&lt;br /&gt;
[http://www.umass.edu/rotellogroup/ Rotello Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Reverse transcriptase|Molecular Playground/Reverse Transcriptase]]&#039;&#039;&#039;, Daniel Moyano-Marino&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Pancreatic Lipase]]&#039;&#039;&#039;,  Rui Tang&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular playground/Chymotrypsin]]&#039;&#039;&#039;,  Brad&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Targeting Peptide]]&#039;&#039;&#039;, David Solfiell&lt;br /&gt;
&lt;br /&gt;
Schnarr Lab &lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[6-deoxyerythronolide_B_synthase_(DEBS)|Molecular Playground/6-Deoxyerythronolide B Synthase]]&#039;&#039;&#039;, Tsung-Yi Lin, Jon Amoroso&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/ACP apo]]&#039;&#039;&#039;, Gitanjeli Prasad&lt;br /&gt;
&lt;br /&gt;
Thayumanavan Lab&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Lysozyme ]]&#039;&#039;&#039;, Daniella Gonzalez&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Beta-galactosidase]]&#039;&#039;&#039;, Judy Ventura&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[User:Krishna Reddy Ragupathi|Molecular Playground/Carbonic Anhydrase]]&#039;&#039;&#039;, Krishna Reddy Raghupathi&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[User:Rami Rajasekhar Reddy|Molecular Playground/Avidin]]&#039;&#039;&#039;, Rami Rajasekar Reddy&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Biotin binding avidin]]&#039;&#039;&#039;, Diego Amado &lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[User:Jiaming Zhuang|Molecular Playground/MMP12]]&#039;&#039;&#039;, Jiaming Zhuang&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039; [[User:Jing Guo|Molecular Playground/Gluconase]]&#039;&#039;&#039;, Jing Guo&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Glutathione Reductase]]&#039;&#039;&#039;, Reuben Chacko&lt;br /&gt;
&lt;br /&gt;
Thayumanavan &amp;amp; Vachet Labs&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Trypsin]]&#039;&#039;&#039;, Gladys Murage&lt;br /&gt;
&lt;br /&gt;
[http://people.chem.umass.edu/thompson/index.html Thompson] &amp;amp; [http://www.chem.umass.edu/~rmweis/weislab/ Weis] Labs&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Bacterial Chemotaxis Receptors]]&#039;&#039;&#039;, Lynmarie K. Thompson, Shiela M. Jones&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/cytoplasmic domain of a serine chemotaxis receptor]]&#039;&#039;&#039;,  Meili Yang&lt;br /&gt;
&lt;br /&gt;
: New Fall 2011 &#039;&#039;&#039;[[Molecular Playground/Cytoplasmic domain of chemoreceptor of Thermotoga maritima]]&#039;&#039;&#039;,  Xuni Li&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[http://www.chem.umass.edu/~vachet/index.html Vachet Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular playground/beta 2 microglobulin]]&#039;&#039;&#039;,  Nick Borotto&lt;br /&gt;
:: Best CBI Molecule Jmol scenes 2010&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/Myoglobin]]&#039;&#039;&#039;,  Yuping Zhou &lt;br /&gt;
&lt;br /&gt;
:&#039;&#039;&#039;[[Molecular Playground/ Copper-Zinc Superoxide Dismutase]]&#039;&#039;&#039;, Shaynah Browne&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Other Molecules of interest&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/PcrA Helicase]]&#039;&#039;&#039;, Luis E Ramirez-Tapia, [http://www.chem.umass.edu/~cmartin/ Martin Lab]&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Other Laboratories&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/YKL-40]]&#039;&#039;&#039;, Ralph A. Francescone III, [http://www.bio.umass.edu/mcb/faculty/Shao.html Shao Lab]&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/BLG|Molecular Playground/β-lactoglobulin]]&#039;&#039;&#039;, Daniel Seeman, Dubin Lab&lt;br /&gt;
&lt;br /&gt;
: &#039;&#039;&#039;[[Molecular Playground/ADAM13]]&#039;&#039;&#039;, Genevieve Abbruzzese, Alfandari Lab&lt;br /&gt;
&lt;br /&gt;
==Instructions==&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;Congratulations to the prize-winning CBI molecules noted above! These also provide great examples to follow. Another prize for best CBI Molecule page and/or scene will be awarded in summer 2012!&#039;&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
Fall 2011: Complete steps 1-4 by 12/1/11, in preparation for the CBI Molecule Workshop.&lt;br /&gt;
&lt;br /&gt;
Choose a molecule that is part of your research project. If someone in your group has already made a page for your research molecule, you can improve on that previous entry. You must leave the previously created page intact and make a copy that you improve and mark as new.  Later we will retain the new one with a merged author list.&lt;br /&gt;
&lt;br /&gt;
1. If you don&#039;t already have one, request a Proteopedia account and log in. If you are new to Proteopedia, click Help in the navigation box on the left to get started.&lt;br /&gt;
&lt;br /&gt;
2. Make yourself a sandbox page in which you will develop your CBI Molecule scene and description  (Enter &amp;quot;User:Your Name/Sandbox 1&amp;quot; (omit quotes) in the search box, then follow instructions to edit this page. See example [[User:Lynmarie K Thompson/Sandbox 1]]). &lt;br /&gt;
&lt;br /&gt;
3. Follow the format of the sample CBI molecule page [[Molecular Playground/Bacterial Chemotaxis Receptors]]. Easiest way to do this is to copy this page (in editing mode), paste it into your sandbox page, keep the first paragraph about CBI molecules, and then edit to describe and display your molecule. Your goal is to make this an interesting, nontechnical description of the molecule. If multiple people in one group work on the same molecule, you can each make different scenes for the same CBI molecule and each describe them on the same proteopedia page. Talk with each other about your plans so you are not duplicating efforts.&lt;br /&gt;
&lt;br /&gt;
4. Add a link to your sandbox page at [[Sandbox_CBI]] (CBI Molecules in Progress).&lt;br /&gt;
&lt;br /&gt;
5. Create an attractive scene for your molecule: use the scene authoring tools in the edit mode to create the view you like, then copy the wiki text into your window.&lt;br /&gt;
&lt;br /&gt;
6. Choose a &amp;quot;green scene&amp;quot; on your Proteopedia page to suggest for display at the Molecular Playground and specify a &amp;quot;banner&amp;quot; which will be projected with the molecule. This should be a short, one-line headline for your scene that includes the name of the molecule and what is important about the scene or the molecule. Remember to design this for the general public, including non-scientists. My example is: &amp;quot;Molecular Playground banner: A bacterial chemotaxis receptor protein used by bacteria to &amp;quot;smell&amp;quot; their environment.&amp;quot;&lt;br /&gt;
&lt;br /&gt;
7. When you are happy with your sandbox page, make yourself a permanent Proteopedia page, which will be editable by others. Enter &amp;quot;Molecular Playground/your molecule&amp;quot; (omit quotes) in the search box, then follow the instructions to create a new page with this title. Copy the content of your sandbox to this new page.&lt;br /&gt;
&lt;br /&gt;
8. When you have finished the final version of your page and scene, edit this CBI Molecules page to add a listing and link for your molecule, following the  examples above, and be sure to mark it as NEW FALL 2011. If you are improving a previously created page, leave the old one intact and make a copy that you improve and mark as new.  Later we will retain the new one with a merged author list. When multiple authors contribute to a Molecular Playground page, please indicate your scene with your initials. Please link the lab names to web pages too.&lt;br /&gt;
&lt;br /&gt;
==Links to HELP pages==&lt;br /&gt;
Videos showing how to use Proteopedia:&lt;br /&gt;
[[Proteopedia:Video_Guide]]&lt;br /&gt;
(Sometimes slow -- if you pause the video and wait awhile it will download and then you can play it without interruptions)&lt;br /&gt;
&lt;br /&gt;
[[Proteopedia:DIY:Scenes|Proteopedia Scenes: Do It Yourself]]&lt;br /&gt;
gives succinct step by step instructions on how to create a molecular scene.&lt;br /&gt;
&lt;br /&gt;
A powerpoint-like set of slides that walks a user through the process of creating a new page and a new molecular scene/green link.&lt;br /&gt;
[http://www.proteopedia.org/wiki/images/1/1b/2009_07_13_Proteopedia_Workshop.pdf Proteopedia Workshop Slides]&lt;br /&gt;
&lt;br /&gt;
[[Proteopedia:Guidelines for Ethical Writing]].&lt;br /&gt;
Please pay attention to the section about images. There are links to examples of images re-used with explicit permission.&lt;br /&gt;
&lt;br /&gt;
For other help resources, click on [[Help:Contents|Help]] in the &#039;&#039;navigation&#039;&#039; box at the upper left of every page in Proteopedia.&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=CBI_Molecules&amp;diff=1082246</id>
		<title>CBI Molecules</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=CBI_Molecules&amp;diff=1082246"/>
		<updated>2010-04-30T21:08:31Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;These are molecules under study by members of the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program].&lt;br /&gt;
Many of the  molecules we study are featured at the [http://www.molecularplayground.org/ Molecular Playground]. Follow the links below to read nontechnical descriptions in Proteopedia.&lt;br /&gt;
&lt;br /&gt;
UMass CBI Members, add your molecules to the list; follow the instructions below the list.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Bacterial Chemotaxis Receptors]]&#039;&#039;&#039;, [http://people.chem.umass.edu/thompson/index.html Thompson] &amp;amp; [http://www.chem.umass.edu/~rmweis/weislab/ Weis] laboratories&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[6-deoxyerythronolide B synthase (DEBS)|Molecular Playground/6-Deoxyerythronolide B Synthase]]&#039;&#039;&#039;, Schnarr lab (Tsung-Yi Lin)&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Lysozime ]]&#039;&#039;&#039;, Daniella Gonzalez, Thayumanavan Research Group&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Beta-galactosidase]]&#039;&#039;&#039;, Judy Ventura, Thayumanavan Research group&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/TRAIL]]&#039;&#039;&#039;, Charley Swofford&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Taxol]]&#039;&#039;&#039;, [http://robertsgroup.ecs.umass.edu/ Roberts Research Group] (Rohan Patil)&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Human Protective Protein Cathepsin A]]&#039;&#039;&#039;, Yadilette Rivera-Colon, [http://www.biochem.umass.edu/garman/index.html Garman Research Group]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/YKL-40]]&#039;&#039;&#039;, Ralph A. Francescone III, [http://www.bio.umass.edu/mcb/faculty/Shao.html Shao Lab]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Reverse transcriptase|Molecular Playground/Reverse Transcriptase]]&#039;&#039;&#039;, Rotello lab (Daniel Moyano-Marino)&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[User:Krishna Reddy Ragupathi|Molecular Playground/Carbonic Anhydrase]]&#039;&#039;&#039;, Thai lab (Krishna Reddy Raghupathi)&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[User:Rami Rajasekhar Reddy|Molecular Playground/Avidin]]&#039;&#039;&#039;, Thai lab (Rami Rajasekar Reddy)&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular_Playground/ERMan1]]&#039;&#039;&#039;, Johan Sunryd&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Insulin]]&#039;&#039;&#039;, [http://robertsgroup.ecs.umass.edu/ Roberts Research Group] (Whitney Stoppel)&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/T7 RNA Polymerase (7 mer int)]]&#039;&#039;&#039;, Ankit Vahia ([http://www.chem.umass.edu/~cmartin/ Martin] lab)&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Human PPCA]]&#039;&#039;&#039;, Nilima Kolli&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Alginate]]&#039;&#039;&#039;, David Griffin&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Glutamate Receptor]]&#039;&#039;&#039;, [http://chamberslab.com/wp/ Chambers Lab] (Amanda Hussey, Steve McCarron, Rosie Combs-Bachmann, Mariel Feliciano)&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Biotin binding avidin]]&#039;&#039;&#039;, Diego Amado&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/FIH]]&#039;&#039;&#039;, Knapp Lab, (Cornelius Taabazuing, Breanne Holmes, John Hangasky)&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[User:Jiaming Zhuang|Molecular Playground/MMP12]]&#039;&#039;&#039;, Jiaming Zhuang&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Pancreatic Lipase]]&#039;&#039;&#039;, [http://www.umass.edu/rotellogroup/ Rotello lab] (Rui Tang)&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Trypsin]]&#039;&#039;&#039;, Thai-Vachet lab (Murage, Gladys)&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular playground/beta 2 microglobulin]]&#039;&#039;&#039;, Vachet lab (Nick)&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Instructions:&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;We plan to award a prize for the best CBI Molecules page and/or scene!&#039;&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
Choose a molecule that is part of your research project.&lt;br /&gt;
&lt;br /&gt;
1. If you don&#039;t already have one, request a Proteopedia account and log in. If you are new to Proteopedia, click Help in the navigation box on the left to get started.&lt;br /&gt;
&lt;br /&gt;
2. Make yourself a sandbox page in which you will develop your CBI Molecule scene and description  (Enter &amp;quot;User:your name/sandbox 1&amp;quot; (omit quotes) in the search box, then follow instructions to edit this page. See example [[User:Lynmarie K Thompson/Sandbox 1]]). &lt;br /&gt;
&lt;br /&gt;
3. Follow the format of the sample CBI molecule page [[Molecular Playground/Bacterial Chemotaxis Receptors]]. Easiest way to do this is to copy this page (in editing mode), paste it into your sandbox page, keep the first paragraph about CBI molecules, and then edit to describe and display your molecule. Your goal is to make this an interesting, nontechnical description of the molecule. If multiple people in one group work on the same molecule, you can each make different scenes for the same CBI molecule and each describe them on the same proteopedia page. Talk with each other about your plans so you are not duplicating efforts.&lt;br /&gt;
&lt;br /&gt;
4. Create an attractive scene for your molecule: use the scene authoring tools in the edit mode to create the view you like, then copy the wiki text into your window.&lt;br /&gt;
&lt;br /&gt;
5. Follow instructions at [[Molecular Playground/Procedures]] as well. But don&#039;t &amp;quot;capture the state script for your scene&amp;quot;; that will be done for you (see #7). With your chosen Jmol scene for the Molecular Playground, specify a &amp;quot;banner&amp;quot;, which will be projected with the molecule on the Molecular Playground. This should be a short, one-line headline for your scene that includes the name of the molecule and what is important about the scene or the molecule. Remember to design this for the general public, including non-scientists. My example is: &amp;quot;Molecular Playground banner: A bacterial chemotaxis receptor protein used by bacteria to &amp;quot;smell&amp;quot; their environment.&amp;quot;&lt;br /&gt;
&lt;br /&gt;
6. When you are happy with your sandbox page, make yourself a permanent Proteopedia page, which will be editable by others. Enter &amp;quot;Molecular Playground/your molecule&amp;quot; (omit quotes) in the search box, then follow the instructions to create a new page with this title. Copy the content of your sandbox to this new page.&lt;br /&gt;
&lt;br /&gt;
7. When you have finished the final version of your page and scene, edit this CBI Molecules page to add a listing and link for your molecule, following the  &amp;quot;Bacterial chemotaxis receptors&amp;quot; example above. Please list your lab group, with your name in parentheses. That way more than one name can be associated with a Molecular Playground page (if there are several students on the Molecular Playground page, please indicate your scene with your initials). It would be great to link the lab names to web pages too. Once this link is there, your scene is considered done, and someone will capture the state script for display on the Molecular Playground.&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=CBI_Molecules&amp;diff=1082243</id>
		<title>CBI Molecules</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=CBI_Molecules&amp;diff=1082243"/>
		<updated>2010-04-30T21:06:26Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;These are molecules under study by members of the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program].&lt;br /&gt;
Many of the  molecules we study are featured at the [http://www.molecularplayground.org/ Molecular Playground]. Follow the links below to read nontechnical descriptions in Proteopedia.&lt;br /&gt;
&lt;br /&gt;
UMass CBI Members, add your molecules to the list; follow the instructions below the list.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Bacterial Chemotaxis Receptors]]&#039;&#039;&#039;, [http://people.chem.umass.edu/thompson/index.html Thompson] &amp;amp; [http://www.chem.umass.edu/~rmweis/weislab/ Weis] laboratories&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[6-deoxyerythronolide B synthase (DEBS)|Molecular Playground/6-Deoxyerythronolide B Synthase]]&#039;&#039;&#039;, Schnarr lab (Tsung-Yi Lin)&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Lysozime ]]&#039;&#039;&#039;, Daniella Gonzalez, Thayumanavan Research Group&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Beta-galactosidase]]&#039;&#039;&#039;, Judy Ventura, Thayumanavan Research group&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/TRAIL]]&#039;&#039;&#039;, Charley Swofford&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Taxol]]&#039;&#039;&#039;, Rohan Patil, [http://robertsgroup.ecs.umass.edu/ Roberts Research Group]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Human Protective Protein Cathepsin A]]&#039;&#039;&#039;, Yadilette Rivera-Colon, [http://www.biochem.umass.edu/garman/index.html Garman Research Group]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/YKL-40]]&#039;&#039;&#039;, Ralph A. Francescone III, [http://www.bio.umass.edu/mcb/faculty/Shao.html Shao Lab]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Reverse transcriptase|Molecular Playground/Reverse Transcriptase]]&#039;&#039;&#039;, Rotello lab (Daniel Moyano-Marino)&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[User:Krishna Reddy Ragupathi|Molecular Playground/Carbonic Anhydrase]]&#039;&#039;&#039;, Thai lab (Krishna Reddy Raghupathi)&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[User:Rami Rajasekhar Reddy|Molecular Playground/Avidin]]&#039;&#039;&#039;, Thai lab (Rami Rajasekar Reddy)&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular_Playground/ERMan1]]&#039;&#039;&#039;, Johan Sunryd&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Insulin]]&#039;&#039;&#039;, Whitney Stoppel, [http://robertsgroup.ecs.umass.edu/ Roberts Research Group]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/T7 RNA Polymerase (7 mer int)]]&#039;&#039;&#039;, Ankit Vahia ([http://www.chem.umass.edu/~cmartin/ Martin] lab)&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Human PPCA]]&#039;&#039;&#039;, Nilima Kolli&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Alginate]]&#039;&#039;&#039;, David Griffin&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Glutamate Receptor]]&#039;&#039;&#039;, [http://chamberslab.com/wp/ Chambers Lab] (Amanda Hussey, Steve McCarron, Rosie Combs-Bachmann, Mariel Feliciano)&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Biotin binding avidin]]&#039;&#039;&#039;, Diego Amado&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/FIH]]&#039;&#039;&#039;, Knapp Lab, (Cornelius Taabazuing, Breanne Holmes, John Hangasky)&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[User:Jiaming Zhuang|Molecular Playground/MMP12]]&#039;&#039;&#039;, Jiaming Zhuang&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Pancreatic Lipase]]&#039;&#039;&#039;, [http://www.umass.edu/rotellogroup/ Rotello lab] (Rui Tang)&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Trypsin]]&#039;&#039;&#039;, Thai-Vachet lab (Murage, Gladys)&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular playground/beta 2 microglobulin]]&#039;&#039;&#039;, Vachet lab (Nick)&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Instructions:&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;We plan to award a prize for the best CBI Molecules page and/or scene!&#039;&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
Choose a molecule that is part of your research project.&lt;br /&gt;
&lt;br /&gt;
1. If you don&#039;t already have one, request a Proteopedia account and log in. If you are new to Proteopedia, click Help in the navigation box on the left to get started.&lt;br /&gt;
&lt;br /&gt;
2. Make yourself a sandbox page in which you will develop your CBI Molecule scene and description  (Enter &amp;quot;User:your name/sandbox 1&amp;quot; (omit quotes) in the search box, then follow instructions to edit this page. See example [[User:Lynmarie K Thompson/Sandbox 1]]). &lt;br /&gt;
&lt;br /&gt;
3. Follow the format of the sample CBI molecule page [[Molecular Playground/Bacterial Chemotaxis Receptors]]. Easiest way to do this is to copy this page (in editing mode), paste it into your sandbox page, keep the first paragraph about CBI molecules, and then edit to describe and display your molecule. Your goal is to make this an interesting, nontechnical description of the molecule. If multiple people in one group work on the same molecule, you can each make different scenes for the same CBI molecule and each describe them on the same proteopedia page. Talk with each other about your plans so you are not duplicating efforts.&lt;br /&gt;
&lt;br /&gt;
4. Create an attractive scene for your molecule: use the scene authoring tools in the edit mode to create the view you like, then copy the wiki text into your window.&lt;br /&gt;
&lt;br /&gt;
5. Follow instructions at [[Molecular Playground/Procedures]] as well. But don&#039;t &amp;quot;capture the state script for your scene&amp;quot;; that will be done for you (see #7). With your chosen Jmol scene for the Molecular Playground, specify a &amp;quot;banner&amp;quot;, which will be projected with the molecule on the Molecular Playground. This should be a short, one-line headline for your scene that includes the name of the molecule and what is important about the scene or the molecule. Remember to design this for the general public, including non-scientists. My example is: &amp;quot;Molecular Playground banner: A bacterial chemotaxis receptor protein used by bacteria to &amp;quot;smell&amp;quot; their environment.&amp;quot;&lt;br /&gt;
&lt;br /&gt;
6. When you are happy with your sandbox page, make yourself a permanent Proteopedia page, which will be editable by others. Enter &amp;quot;Molecular Playground/your molecule&amp;quot; (omit quotes) in the search box, then follow the instructions to create a new page with this title. Copy the content of your sandbox to this new page.&lt;br /&gt;
&lt;br /&gt;
7. When you have finished the final version of your page and scene, edit this CBI Molecules page to add a listing and link for your molecule, following the  &amp;quot;Bacterial chemotaxis receptors&amp;quot; example above. Please list your lab group, with your name in parentheses. That way more than one name can be associated with a Molecular Playground page (if there are several students on the Molecular Playground page, please indicate your scene with your initials). It would be great to link the lab names to web pages too. Once this link is there, your scene is considered done, and someone will capture the state script for display on the Molecular Playground.&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Molecular_Playground/Insulin&amp;diff=1082172</id>
		<title>Molecular Playground/Insulin</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Molecular_Playground/Insulin&amp;diff=1082172"/>
		<updated>2010-04-30T19:36:21Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the CBI Molecules being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst in the [http://robertsgroup.ecs.umass.edu/ Roberts Research Group] and on display at the [http://www.molecularplayground.org Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;applet size=&#039;[450,338]&#039; frame=&#039;true&#039; align=&#039;right&#039;&lt;br /&gt;
caption=&#039;Insulin&#039; /&amp;gt; &amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Human_insulin2/1&#039;&amp;gt;Insulin&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;Molecular Playground banner: Insulin is used by the body to regulate blood sugar.&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Insulin is made up of two pieces called the A- and B-chain, shown above in blue and green respectively.  These two chains are joined by disulfide bonds, which are shown in yellow.  This single piece made up of the A- and B-chains is the active form of the insulin hormone.  This is the form that binds the insulin receptor on fat or muscle cells in the body, singling them to take up glucose, or sugar, from the blood and save it for later.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_dimer/2&#039;&amp;gt;Hydrogen Bonding in an Insulin Dimer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;Molecular Playground banner: Insulin is able to make &amp;quot;pairs&amp;quot; or dimers by connecting two B-chains with hydrogen bonds.&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Insulin is able to pair-up with itself and form a dimer by forming hydrogen bonds between the ends of two B-chains.  These hydrogen bonds are shown above in white.  Then, 3 dimers can come together in the presence of zinc ions and form a hexamer.  Insulin is stored in the hexameric form in the body.       &lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_hexamer/4&#039;&amp;gt;Symmetric Insulin Hexamer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;Molecular Playground banner: Insulin is stored in the body in groups of 6, an called Insulin Hexamer.&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Insulin is a hormone that controls sugar metabolism and storage in the human body.  The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.  Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes.  The image below highlights the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7.  It is believed that the hydrophobic sections on the B-chain cause insulin aggregation which initially caused problems in the manufacture and storage of insulin for pharmaceutical use.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_ph7/2&#039;&amp;gt;Insulin monomer at pH 7&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1082170</id>
		<title>User:Whitney Stoppel/sandbox1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1082170"/>
		<updated>2010-04-30T19:34:16Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the CBI Molecules being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst in the [http://robertsgroup.ecs.umass.edu/ Roberts Research Group] and on display at the [http://www.molecularplayground.org Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&amp;lt;applet size=&#039;[450,338]&#039; frame=&#039;true&#039; align=&#039;right&#039;&lt;br /&gt;
caption=&#039;Insulin, showing disulfide bridges between the A-chain and B-chain&#039; /&amp;gt; &amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Human_insulin2/1&#039;&amp;gt;Insulin&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is made up of two pieces called the A- and B-chain, shown above in blue and green respectively.  These two chains are joined by disulfide bonds, which are shown in yellow.  This single piece made up of the A- and B-chains is the active form of the insulin hormone.  This is the form that binds the insulin receptor on fat or muscle cells in the body, singling them to take up glucose, or sugar, from the blood and save it for later.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_dimer/2&#039;&amp;gt;Hydrogen Bonding in an Insulin Dimer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is able to pair-up with itself and form a dimer by forming hydrogen bonds between the ends of two B-chains.  These hydrogen bonds are shown above in white.  Then, 3 dimers can come together in the presence of zinc ions and form a hexamer.  Insulin is stored in the hexameric form in the body.       &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_hexamer/4&#039;&amp;gt;Symmetric Insulin Hexamer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is a hormone that controls sugar metabolism and storage in the human body.  The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.  Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes.  The image below highlights the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7.  It is believed that the hydrophobic sections on the B-chain cause insulin aggregation which initially caused problems in the manufacture and storage of insulin for pharmaceutical use.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_ph7/2&#039;&amp;gt;Insulin monomer at pH 7&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Molecular_Playground/Insulin&amp;diff=1082159</id>
		<title>Molecular Playground/Insulin</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Molecular_Playground/Insulin&amp;diff=1082159"/>
		<updated>2010-04-30T19:12:49Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the CBI Molecules being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst in the [http://robertsgroup.ecs.umass.edu/ Roberts Research Group] and on display at the [http://www.molecularplayground.org Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;applet size=&#039;[450,338]&#039; frame=&#039;true&#039; align=&#039;right&#039;&lt;br /&gt;
caption=&#039;Insulin&#039; /&amp;gt; &amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Human_insulin2/1&#039;&amp;gt;Insulin&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;Molecular Playground banner: Insulin is used by the body to regulate blood sugar.&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Insulin is made up of two pieces called the A- and B-chain, shown above in blue and green respectively.  These two chains are joined by disulfide bonds, which are shown in yellow.  This single piece made up of the A- and B-chains is the active form of the insulin hormone.  This is the form that binds the insulin receptor on fat or muscle cells in the body, singling them to take up glucose, or sugar, from the blood and save it for later.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_dimer/2&#039;&amp;gt;Hydrogen Bonding in an Insulin Dimer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;Molecular Playground banner: Insulin is able to make &amp;quot;pairs&amp;quot; or dimers by connecting two B-chains with hydrogen bonds.&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Insulin is able to pair-up with itself and form a dimer by forming hydrogen bonds between the ends of two B-chains.  These hydrogen bonds are shown above in white.  Then, 3 dimers can come together in the presence of zinc ions and form a hexamer.  Insulin is stored in the hexameric form in the body.       &lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_hexamer/3&#039;&amp;gt;Symmetric Insulin Hexamer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;Molecular Playground banner: Insulin is stored in the body in groups of 6, an called Insulin Hexamer.&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Insulin is a hormone that controls sugar metabolism and storage in the human body.  The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.  Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes.  The image below highlights the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7.  It is believed that the hydrophobic sections on the B-chain cause insulin aggregation which initially caused problems in the manufacture and storage of insulin for pharmaceutical use.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_ph7/2&#039;&amp;gt;Insulin monomer at pH 7&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Molecular_Playground/Insulin&amp;diff=1082154</id>
		<title>Molecular Playground/Insulin</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Molecular_Playground/Insulin&amp;diff=1082154"/>
		<updated>2010-04-30T19:05:48Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the CBI Molecules being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst in the [http://robertsgroup.ecs.umass.edu/ Roberts Research Group] and on display at the [http://www.molecularplayground.org Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;applet size=&#039;[450,338]&#039; frame=&#039;true&#039; align=&#039;right&#039;&lt;br /&gt;
caption=&#039;Insulin&#039; /&amp;gt; &amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Human_insulin2/1&#039;&amp;gt;Insulin&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;Molecular Playground banner: Insulin is used by the body to regulate blood sugar.&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Insulin is made up of two pieces called the A- and B-chain, shown above in blue and green respectively.  These two chains are joined by disulfide bonds, which are shown in yellow.  This single piece made up of the A- and B-chains is the active form of the insulin hormone.  This is the form that binds the insulin receptor on fat or muscle cells in the body, singling them to take up glucose, or sugar, from the blood and save it for later.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_dimer/2&#039;&amp;gt;Hydrogen Bonding in an Insulin Dimer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Insulin is able to pair-up with itself and form a dimer by forming hydrogen bonds between the ends of two B-chains.  These hydrogen bonds are shown above in white.  Then, 3 dimers can come together in the presence of zinc ions and form a hexamer.  Insulin is stored in the hexameric form in the body.       &lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_hexamer/3&#039;&amp;gt;Symmetric Insulin Hexamer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;Molecular Playground banner: Insulin is stored in the body in groups of 6, an called Insulin Hexamer.&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Insulin is a hormone that controls sugar metabolism and storage in the human body.  The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.  Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes.  The image below highlights the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7.  It is believed that the hydrophobic sections on the B-chain cause insulin aggregation which initially caused problems in the manufacture and storage of insulin for pharmaceutical use.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_ph7/2&#039;&amp;gt;Insulin monomer at pH 7&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Molecular_Playground/Insulin&amp;diff=1082151</id>
		<title>Molecular Playground/Insulin</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Molecular_Playground/Insulin&amp;diff=1082151"/>
		<updated>2010-04-30T19:04:39Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the CBI Molecules being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst in the [http://robertsgroup.ecs.umass.edu/ Roberts Research Group] and on display at the [http://www.molecularplayground.org Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;applet size=&#039;[450,338]&#039; frame=&#039;true&#039; align=&#039;right&#039;&lt;br /&gt;
caption=&#039;Insulin, showing disulfide bridges between the A-chain and B-chain&#039; /&amp;gt; &amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Human_insulin2/1&#039;&amp;gt;Insulin&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;Molecular Playground banner: Insulin is used by the body to regulate blood sugar.&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Insulin is made up of two pieces called the A- and B-chain, shown above in blue and green respectively.  These two chains are joined by disulfide bonds, which are shown in yellow.  This single piece made up of the A- and B-chains is the active form of the insulin hormone.  This is the form that binds the insulin receptor on fat or muscle cells in the body, singling them to take up glucose, or sugar, from the blood and save it for later.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_dimer/2&#039;&amp;gt;Hydrogen Bonding in an Insulin Dimer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Insulin is able to pair-up with itself and form a dimer by forming hydrogen bonds between the ends of two B-chains.  These hydrogen bonds are shown above in white.  Then, 3 dimers can come together in the presence of zinc ions and form a hexamer.  Insulin is stored in the hexameric form in the body.       &lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_hexamer/3&#039;&amp;gt;Symmetric Insulin Hexamer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;Molecular Playground banner: Insulin is stored in the body in groups of 6, an called Insulin Hexamer.&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Insulin is a hormone that controls sugar metabolism and storage in the human body.  The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.  Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes.  The image below highlights the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7.  It is believed that the hydrophobic sections on the B-chain cause insulin aggregation which initially caused problems in the manufacture and storage of insulin for pharmaceutical use.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_ph7/2&#039;&amp;gt;Insulin monomer at pH 7&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Molecular_Playground/Insulin&amp;diff=1082150</id>
		<title>Molecular Playground/Insulin</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Molecular_Playground/Insulin&amp;diff=1082150"/>
		<updated>2010-04-30T19:04:13Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the CBI Molecules being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst in the [http://robertsgroup.ecs.umass.edu/ Roberts Research Group] and on display at the [http://www.molecularplayground.org Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&amp;lt;applet size=&#039;[450,338]&#039; frame=&#039;true&#039; align=&#039;right&#039;&lt;br /&gt;
caption=&#039;Insulin, showing disulfide bridges between the A-chain and B-chain&#039; /&amp;gt; &amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Human_insulin2/1&#039;&amp;gt;Insulin&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;Molecular Playground banner: Insulin is used by the body to regulate blood sugar.&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Insulin is made up of two pieces called the A- and B-chain, shown above in blue and green respectively.  These two chains are joined by disulfide bonds, which are shown in yellow.  This single piece made up of the A- and B-chains is the active form of the insulin hormone.  This is the form that binds the insulin receptor on fat or muscle cells in the body, singling them to take up glucose, or sugar, from the blood and save it for later.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_dimer/2&#039;&amp;gt;Hydrogen Bonding in an Insulin Dimer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Insulin is able to pair-up with itself and form a dimer by forming hydrogen bonds between the ends of two B-chains.  These hydrogen bonds are shown above in white.  Then, 3 dimers can come together in the presence of zinc ions and form a hexamer.  Insulin is stored in the hexameric form in the body.       &lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_hexamer/3&#039;&amp;gt;Symmetric Insulin Hexamer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;Molecular Playground banner: Insulin is stored in the body in groups of 6, an called Insulin Hexamer.&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Insulin is a hormone that controls sugar metabolism and storage in the human body.  The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.  Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes.  The image below highlights the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7.  It is believed that the hydrophobic sections on the B-chain cause insulin aggregation which initially caused problems in the manufacture and storage of insulin for pharmaceutical use.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_ph7/2&#039;&amp;gt;Insulin monomer at pH 7&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=CBI_Molecules&amp;diff=1082005</id>
		<title>CBI Molecules</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=CBI_Molecules&amp;diff=1082005"/>
		<updated>2010-04-30T14:26:18Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;These are molecules under study by members of the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program].&lt;br /&gt;
Many of the  molecules we study are featured at the [http://www.molecularplayground.org/ Molecular Playground]. Follow the links below to read nontechnical descriptions in Proteopedia.&lt;br /&gt;
&lt;br /&gt;
UMass CBI Members, add your molecules to the list; follow the instructions below the list.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Bacterial Chemotaxis Receptors]]&#039;&#039;&#039;, Thompson &amp;amp; Weis laboratories&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[User:Tsung-Yi_Lin/6-deoxyerythronolide_B_synthase|Molecular Playground/6-Deoxyerythronolide B Synthase]]&#039;&#039;&#039;, Tsung-Yi Lin&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Lysozime ]]&#039;&#039;&#039;, Daniella Gonzalez&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Beta-galactosidase]]&#039;&#039;&#039;, Judy Ventura&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/TRAIL]]&#039;&#039;&#039;, Charley Swofford&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Taxol]]&#039;&#039;&#039;, Rohan Patil&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Human Protective Protein Cathepsin A]]&#039;&#039;&#039;, Yadilette Rivera-Colon&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/YKL-40]]&#039;&#039;&#039;, Ralph A. Francescone III&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Reverse transcriptase|Molecular Playground/Reverse Transcriptase]]&#039;&#039;&#039;, Rotello lab (Daniel Moyano-Marino)&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[User:Krishna Reddy Ragupathi|Molecular Playground/Carbonic Anhydrase]]&#039;&#039;&#039;, Krishna Reddy Raghupathi&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[User:Rami Rajasekhar Reddy|Molecular Playground/Avidin]]&#039;&#039;&#039;, Rami Rajasekar Reddy&lt;br /&gt;
&lt;br /&gt;
[http://proteopedia.org/wiki/index.php/Molecular_Playground/ERMan1], Johan Sunryd&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;[[Molecular Playground/Insulin]]&#039;&#039;&#039;, Whitney Stoppel&lt;br /&gt;
&lt;br /&gt;
Instructions:&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;We plan to award a prize for the best CBI Molecules page and/or scene!&#039;&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
Choose a molecule that is part of your research project.&lt;br /&gt;
&lt;br /&gt;
1. If you don&#039;t already have one, request a Proteopedia account and log in. If you are new to Proteopedia, click Help in the navigation box on the left to get started.&lt;br /&gt;
&lt;br /&gt;
2. Make yourself a sandbox page in which you will develop your CBI Molecule scene and description  (Enter &amp;quot;User:your name/sandbox 1&amp;quot; (omit quotes) in the search box, then follow instructions to edit this page. See example [[User:Lynmarie K Thompson/Sandbox 1]]). &lt;br /&gt;
&lt;br /&gt;
3. Follow the format of the sample CBI molecule page [[Molecular Playground/Bacterial Chemotaxis Receptors]]. Easiest way to do this is to copy this page (in editing mode), paste it into your sandbox page, keep the first paragraph about CBI molecules, and then edit to describe and display your molecule. Your goal is to make this an interesting, nontechnical description of the molecule. If multiple people in one group work on the same molecule, you can each make different scenes for the same CBI molecule and each describe them on the same proteopedia page. Talk with each other about your plans so you are not duplicating efforts.&lt;br /&gt;
&lt;br /&gt;
4. Create an attractive scene for your molecule: use the scene authoring tools in the edit mode to create the view you like, then copy the wiki text into your window.&lt;br /&gt;
&lt;br /&gt;
5. Follow instructions at [[Molecular Playground/Procedures]] as well. But don&#039;t &amp;quot;capture the state script for your scene&amp;quot;; that will be done for you (see #7).&lt;br /&gt;
&lt;br /&gt;
6. When you are happy with your sandbox page, make yourself a permanent Proteopedia page, which will be editable by others. Enter &amp;quot;Molecular Playground/your molecule&amp;quot; (omit quotes) in the search box, then follow the instructions to create a new page with this title. Copy the content of your sandbox to this new page.&lt;br /&gt;
&lt;br /&gt;
7. When you have finished the final version of your page and scene, edit this CBI Molecules page to add a listing and link for your molecule, following the  &amp;quot;Bacterial chemotaxis receptors&amp;quot; example above. Once this link is there, your scene is considered done, and someone will capture the state script for display on the Molecular Playground.&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Molecular_Playground/Insulin&amp;diff=1082004</id>
		<title>Molecular Playground/Insulin</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Molecular_Playground/Insulin&amp;diff=1082004"/>
		<updated>2010-04-30T14:23:27Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: New page: One of the CBI Molecules being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst in the [http://robertsgro...&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the CBI Molecules being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst in the [http://robertsgroup.ecs.umass.edu/ Roberts Research Group] and on display at the [http://www.molecularplayground.org Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&amp;lt;applet size=&#039;[450,338]&#039; frame=&#039;true&#039; align=&#039;right&#039;&lt;br /&gt;
caption=&#039;Insulin, showing disulfide bridges between the A-chain and B-chain&#039; /&amp;gt; &amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Human_insulin2/1&#039;&amp;gt;Insulin&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is made up of two pieces called the A- and B-chain, shown above in blue and green respectively.  These two chains are joined by disulfide bonds, which are shown in yellow.  This single piece made up of the A- and B-chains is the active form of the insulin hormone.  This is the form that binds the insulin receptor on fat or muscle cells in the body, singling them to take up glucose, or sugar, from the blood and save it for later.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_dimer/2&#039;&amp;gt;Hydrogen Bonding in an Insulin Dimer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is able to pair-up with itself and form a dimer by forming hydrogen bonds between the ends of two B-chains.  These hydrogen bonds are shown above in white.  Then, 3 dimers can come together in the presence of zinc ions and form a hexamer.  Insulin is stored in the hexameric form in the body.       &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_hexamer/3&#039;&amp;gt;Symmetric Insulin Hexamer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is a hormone that controls sugar metabolism and storage in the human body.  The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.  Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes.  The image below highlights the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7.  It is believed that the hydrophobic sections on the B-chain cause insulin aggregation which initially caused problems in the manufacture and storage of insulin for pharmaceutical use.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_ph7/2&#039;&amp;gt;Insulin monomer at pH 7&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1082000</id>
		<title>User:Whitney Stoppel/sandbox1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1082000"/>
		<updated>2010-04-30T14:18:48Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the CBI Molecules being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst in the [http://robertsgroup.ecs.umass.edu/ Roberts Research Group] and on display at the [http://www.molecularplayground.org Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&amp;lt;applet size=&#039;[450,338]&#039; frame=&#039;true&#039; align=&#039;right&#039;&lt;br /&gt;
caption=&#039;Insulin, showing disulfide bridges between the A-chain and B-chain&#039; /&amp;gt; &amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Human_insulin2/1&#039;&amp;gt;Insulin&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is made up of two pieces called the A- and B-chain, shown above in blue and green respectively.  These two chains are joined by disulfide bonds, which are shown in yellow.  This single piece made up of the A- and B-chains is the active form of the insulin hormone.  This is the form that binds the insulin receptor on fat or muscle cells in the body, singling them to take up glucose, or sugar, from the blood and save it for later.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_dimer/2&#039;&amp;gt;Hydrogen Bonding in an Insulin Dimer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is able to pair-up with itself and form a dimer by forming hydrogen bonds between the ends of two B-chains.  These hydrogen bonds are shown above in white.  Then, 3 dimers can come together in the presence of zinc ions and form a hexamer.  Insulin is stored in the hexameric form in the body.       &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_hexamer/3&#039;&amp;gt;Symmetric Insulin Hexamer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is a hormone that controls sugar metabolism and storage in the human body.  The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.  Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes.  The image below highlights the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7.  It is believed that the hydrophobic sections on the B-chain cause insulin aggregation which initially caused problems in the manufacture and storage of insulin for pharmaceutical use.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_ph7/2&#039;&amp;gt;Insulin monomer at pH 7&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081996</id>
		<title>User:Whitney Stoppel/sandbox1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081996"/>
		<updated>2010-04-30T14:17:18Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the CBI Molecules being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst in the [http://robertsgroup.ecs.umass.edu/ Roberts Research Group] and on display at the [http://www.molecularplayground.org Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&amp;lt;applet size=&#039;[450,338]&#039; frame=&#039;true&#039; align=&#039;right&#039;&lt;br /&gt;
caption=&#039;Insulin, showing disulfide bridges between the A-chain and B-chain&#039; /&amp;gt; &amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Human_insulin2/1&#039;&amp;gt;Insulin&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Insulin is made up of two pieces called the A- and B-chain, shown above in blue and green respectively.  These two chains are joined by disulfide bonds, which are shown in yellow.  This single piece made up of the A- and B-chains is the active form of the insulin hormone.  This is the form that binds the insulin receptor on fat or muscle cells in the body, singling them to take up glucose, or sugar, from the blood and save it for later.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;applet size=&#039;[450,338]&#039; frame=&#039;true&#039; align=&#039;right&#039;&lt;br /&gt;
caption=&#039;Insulin dimer, with hydrogen bonding shown in white&#039; /&amp;gt; &amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_dimer/2&#039;&amp;gt;Hydrogen Bonding in an Insulin Dimer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Insulin is able to pair-up with itself and form a dimer by forming hydrogen bonds between the ends of two B-chains.  These hydrogen bonds are shown above in white.  Then, 3 dimers can come together in the presence of zinc ions and form a hexamer.  Insulin is stored in the hexameric form in the body.       &lt;br /&gt;
&lt;br /&gt;
&amp;lt;applet size=&#039;[450,338]&#039; frame=&#039;true&#039; align=&#039;right&#039;&lt;br /&gt;
caption=&#039;Symmetric insulin hexamer with zinc ions shown&#039; /&amp;gt; &amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_hexamer/3&#039;&amp;gt;Symmetric Insulin Hexamer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Insulin is a hormone that controls sugar metabolism and storage in the human body.  The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.  Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes.  The image below highlights the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7.  It is believed that the hydrophobic sections on the B-chain cause insulin aggregation which initially caused problems in the manufacture and storage of insulin for pharmaceutical use.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;applet size=&#039;[450,338]&#039; frame=&#039;true&#039; align=&#039;right&#039;&lt;br /&gt;
caption=&#039;Insulin monomer at pH 7 with hydrophobic sections shown in gray&#039; /&amp;gt; &amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_ph7/2&#039;&amp;gt;Insulin monomer at pH 7&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081995</id>
		<title>User:Whitney Stoppel/sandbox1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081995"/>
		<updated>2010-04-30T14:16:30Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the CBI Molecules being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst in the [http://robertsgroup.ecs.umass.edu/ Roberts Research Group] and on display at the [http://www.molecularplayground.org Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&amp;lt;applet size=&#039;[450,338]&#039; frame=&#039;true&#039; align=&#039;right&#039;&lt;br /&gt;
caption=&#039;Insulin, showing disulfide bridges between the A-chain and B-chain&#039; /&amp;gt; &amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Human_insulin2/1&#039;&amp;gt;Insulin&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is made up of two pieces called the A- and B-chain, shown above in blue and green respectively.  These two chains are joined by disulfide bonds, which are shown in yellow.  This single piece made up of the A- and B-chains is the active form of the insulin hormone.  This is the form that binds the insulin receptor on fat or muscle cells in the body, singling them to take up glucose, or sugar, from the blood and save it for later.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;applet size=&#039;[450,338]&#039; frame=&#039;true&#039; align=&#039;right&#039;&lt;br /&gt;
caption=&#039;Insulin dimer, with hydrogen bonding shown in white&#039; /&amp;gt; &amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_dimer/2&#039;&amp;gt;Hydrogen Bonding in an Insulin Dimer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is able to pair-up with itself and form a dimer by forming hydrogen bonds between the ends of two B-chains.  These hydrogen bonds are shown above in white.  Then, 3 dimers can come together in the presence of zinc ions and form a hexamer.  Insulin is stored in the hexameric form in the body.       &lt;br /&gt;
&lt;br /&gt;
&amp;lt;applet size=&#039;[450,338]&#039; frame=&#039;true&#039; align=&#039;right&#039;&lt;br /&gt;
caption=&#039;Symmetric insulin hexamer with zinc ions shown&#039; /&amp;gt; &amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_hexamer/3&#039;&amp;gt;Symmetric Insulin Hexamer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is a hormone that controls sugar metabolism and storage in the human body.  The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.  Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes.  The image below highlights the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7.  It is believed that the hydrophobic sections on the B-chain cause insulin aggregation which initially caused problems in the manufacture and storage of insulin for pharmaceutical use.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;applet size=&#039;[450,338]&#039; frame=&#039;true&#039; align=&#039;right&#039;&lt;br /&gt;
caption=&#039;Insulin monomer at pH 7 with hydrophobic sections shown in gray&#039; /&amp;gt; &amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_ph7/2&#039;&amp;gt;Insulin monomer at pH 7&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081994</id>
		<title>User:Whitney Stoppel/sandbox1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081994"/>
		<updated>2010-04-30T14:11:20Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the CBI Molecules being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst in the [http://robertsgroup.ecs.umass.edu/ Roberts Research Group] and on display at the [http://www.molecularplayground.org Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&amp;lt;applet size=&#039;[450,338]&#039; frame=&#039;true&#039; align=&#039;right&#039;&lt;br /&gt;
caption=&#039;Insulin, showing hydrogen bonding between the A-chain and B-chain&#039; /&amp;gt; &amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Human_insulin2/1&#039;&amp;gt;Insulin&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is made up of two pieces called the A- and B-chain, shown above in blue and green respectively.  These two chains are joined by disulfide bonds, which are shown in yellow.  This single piece made up of the A- and B-chains is the active form of the insulin hormone.  This is the form that binds the insulin receptor on fat or muscle cells in the body, singling them to take up glucose, or sugar, from the blood and save it for later.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_dimer/2&#039;&amp;gt;Hydrogen Bonding in an Insulin Dimer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is able to pair-up with itself and form a dimer by forming hydrogen bonds between the ends of two B-chains.  These hydrogen bonds are shown above in white.  Then, 3 dimers can come together in the presence of zinc ions and form a hexamer.  Insulin is stored in the hexameric form in the body.       &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_hexamer/3&#039;&amp;gt;Symmetric Insulin Hexamer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is a hormone that controls sugar metabolism and storage in the human body.  The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.  Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes.  The image below highlights the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7.  It is believed that the hydrophobic sections on the B-chain cause insulin aggregation which initially caused problems in the manufacture and storage of insulin for pharmaceutical use.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_ph7/2&#039;&amp;gt;Insulin monomer at pH 7&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081993</id>
		<title>User:Whitney Stoppel/sandbox1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081993"/>
		<updated>2010-04-30T14:07:21Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the CBI Molecules being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst in the [http://robertsgroup.ecs.umass.edu/ Roberts Research Group] and on display at the [http://www.molecularplayground.org Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&amp;lt;applet load=&#039;1wat&#039; size=&#039;[450,338]&#039; frame=&#039;true&#039; align=&#039;right&#039;&lt;br /&gt;
caption=&#039;Insulin, showing hydrogen bonding between the A-chain and B-chain&#039; scene=&#039;User:Whitney_Stoppel/sandbox1/Human_insulin2/1&#039;&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is made up of two pieces called the A- and B-chain, shown above in blue and green respectively.  These two chains are joined by disulfide bonds, which are shown in yellow.  This single piece made up of the A- and B-chains is the active form of the insulin hormone.  This is the form that binds the insulin receptor on fat or muscle cells in the body, singling them to take up glucose, or sugar, from the blood and save it for later.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_dimer/2&#039;&amp;gt;Hydrogen Bonding in an Insulin Dimer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is able to pair-up with itself and form a dimer by forming hydrogen bonds between the ends of two B-chains.  These hydrogen bonds are shown above in white.  Then, 3 dimers can come together in the presence of zinc ions and form a hexamer.  Insulin is stored in the hexameric form in the body.       &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_hexamer/3&#039;&amp;gt;Symmetric Insulin Hexamer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is a hormone that controls sugar metabolism and storage in the human body.  The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.  Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes.  The image below highlights the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7.  It is believed that the hydrophobic sections on the B-chain cause insulin aggregation which initially caused problems in the manufacture and storage of insulin for pharmaceutical use.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_ph7/2&#039;&amp;gt;Insulin monomer at pH 7&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081916</id>
		<title>User:Whitney Stoppel/sandbox1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081916"/>
		<updated>2010-04-30T00:34:17Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the CBI Molecules being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst in the [http://robertsgroup.ecs.umass.edu/ Roberts Research Group] and on display at the [http://www.molecularplayground.org Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Human_insulin2/1&#039;&amp;gt;Insulin&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is made up of two pieces called the A- and B-chain, shown above in blue and green respectively.  These two chains are joined by disulfide bonds, which are shown in yellow.  This single piece made up of the A- and B-chains is the active form of the insulin hormone.  This is the form that binds the insulin receptor on fat or muscle cells in the body, singling them to take up glucose, or sugar, from the blood and save it for later.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_dimer/2&#039;&amp;gt;Hydrogen Bonding in an Insulin Dimer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is able to pair-up with itself and form a dimer by forming hydrogen bonds between the ends of two B-chains.  These hydrogen bonds are shown above in white.  Then, 3 dimers can come together in the presence of zinc ions and form a hexamer.  Insulin is stored in the hexameric form in the body.       &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_hexamer/3&#039;&amp;gt;Symmetric Insulin Hexamer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is a hormone that controls sugar metabolism and storage in the human body.  The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.  Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes.  The image below highlights the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7.  It is believed that the hydrophobic sections on the B-chain cause insulin aggregation which initially caused problems in the manufacture and storage of insulin for pharmaceutical use.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_ph7/2&#039;&amp;gt;Insulin monomer at pH 7&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081915</id>
		<title>User:Whitney Stoppel/sandbox1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081915"/>
		<updated>2010-04-30T00:32:57Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the CBI Molecules being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst in the [http://robertsgroup.ecs.umass.edu/ Roberts Research Group] and on display at the [http://www.molecularplayground.org Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&amp;lt;applet load=&#039;&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Human_insulin2/1&#039;&amp;gt;Insulin&amp;lt;/scene&amp;gt;&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;Human Insulin&#039; /&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is made up of two pieces called the A- and B-chain, shown above in blue and green respectively.  These two chains are joined by disulfide bonds, which are shown in yellow.  This single piece made up of the A- and B-chains is the active form of the insulin hormone.  This is the form that binds the insulin receptor on fat or muscle cells in the body, singling them to take up glucose, or sugar, from the blood and save it for later.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_dimer/2&#039;&amp;gt;Hydrogen Bonding in an Insulin Dimer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is able to pair-up with itself and form a dimer by forming hydrogen bonds between the ends of two B-chains.  These hydrogen bonds are shown above in white.  Then, 3 dimers can come together in the presence of zinc ions and form a hexamer.  Insulin is stored in the hexameric form in the body.       &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_hexamer/3&#039;&amp;gt;Symmetric Insulin Hexamer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is a hormone that controls sugar metabolism and storage in the human body.  The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.  Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes.  The image below highlights the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7.  It is believed that the hydrophobic sections on the B-chain cause insulin aggregation which initially caused problems in the manufacture and storage of insulin for pharmaceutical use.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_ph7/2&#039;&amp;gt;Insulin monomer at pH 7&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081912</id>
		<title>User:Whitney Stoppel/sandbox1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081912"/>
		<updated>2010-04-30T00:27:16Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the CBI Molecules being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst in the [http://robertsgroup.ecs.umass.edu/ Roberts Research Group] and on display at the [http://www.molecularplayground.org Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Human_insulin2/1&#039;&amp;gt;Insulin&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is made up of two pieces called the A- and B-chain, shown above in blue and green respectively.  These two chains are joined by disulfide bonds, which are shown in yellow.  This single piece made up of the A- and B-chains is the active form of the insulin hormone.  This is the form that binds the insulin receptor on fat or muscle cells in the body, singling them to take up glucose, or sugar, from the blood and save it for later.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_dimer/2&#039;&amp;gt;Hydrogen Bonding in an Insulin Dimer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is able to pair-up with itself and form a dimer by forming hydrogen bonds between the ends of two B-chains.  These hydrogen bonds are shown above in white.  Then, 3 dimers can come together in the presence of zinc ions and form a hexamer.  Insulin is stored in the hexameric form in the body.       &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_hexamer/3&#039;&amp;gt;Symmetric Insulin Hexamer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is a hormone that controls sugar metabolism and storage in the human body.  The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.  Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes.  The image below highlights the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7.  It is believed that the hydrophobic sections on the B-chain cause insulin aggregation which initially caused problems in the manufacture and storage of insulin for pharmaceutical use.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_ph7/2&#039;&amp;gt;Insulin monomer at pH 7&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081908</id>
		<title>User:Whitney Stoppel/sandbox1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081908"/>
		<updated>2010-04-30T00:23:51Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the CBI Molecules being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst in the [http://robertsgroup.ecs.umass.edu/ Roberts Research Group] and on display at the [http://www.molecularplayground.org Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Human_insulin2/1&#039;&amp;gt;Insulin&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is made up of two pieces called the A- and B-chain, shown above in blue and green respectively.  These two chains are joined by disulfide bonds, which are shown in yellow.  This single piece made up of the A- and B-chains is the active form of the insulin hormone.  This is the form that binds the insulin receptor on fat or muscle cells in the body, singling them to take up glucose, or sugar, from the blood and save it for later.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_dimer/2&#039;&amp;gt;Hydrogen Bonding in an Insulin Dimer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is able to pair-up with itself and form a dimer by forming hydrogen bonds between the ends of two B-chains.  These hydrogen bonds are shown above in white.  Then, 3 dimers can come together in the presence of zinc ions and form a hexamer.  Insulin is stored in the hexameric form in the body.       &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_hexamer/2&#039;&amp;gt;Symmetric Insulin Hexamer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is a hormone that controls sugar metabolism and storage in the human body.  The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.  Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes.  The image below highlights the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7.  It is believed that the hydrophobic sections on the B-chain cause insulin aggregation which initially caused problems in the manufacture and storage of insulin for pharmaceutical use.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_ph7/1&#039;&amp;gt;Insulin: pH 7&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081907</id>
		<title>User:Whitney Stoppel/sandbox1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081907"/>
		<updated>2010-04-30T00:23:02Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the CBI Molecules being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst in the [http://robertsgroup.ecs.umass.edu/ Roberts Research Group] and on display at the [http://www.molecularplayground.org Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Human_insulin2/1&#039;&amp;gt;Insulin Dimer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is made up of two pieces called the A- and B-chain, shown above in blue and green respectively.  These two chains are joined by disulfide bonds, which are shown in yellow.  This single piece made up of the A- and B-chains is the active form of the insulin hormone.  This is the form that binds the insulin receptor on fat or muscle cells in the body, singling them to take up glucose, or sugar, from the blood and save it for later.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_dimer/2&#039;&amp;gt;TextToBeDisplayed&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is able to pair-up with itself and form a dimer by forming hydrogen bonds between the ends of two B-chains.  These hydrogen bonds are shown above in white.  Then, 3 dimers can come together in the presence of zinc ions and form a hexamer.  Insulin is stored in the hexameric form in the body.       &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_hexamer/2&#039;&amp;gt;Symmetric Insulin Hexamer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is a hormone that controls sugar metabolism and storage in the human body.  The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.  Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes.  The image below highlights the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7.  It is believed that the hydrophobic sections on the B-chain cause insulin aggregation which initially caused problems in the manufacture and storage of insulin for pharmaceutical use.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_ph7/1&#039;&amp;gt;Insulin: pH 7&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081904</id>
		<title>User:Whitney Stoppel/sandbox1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081904"/>
		<updated>2010-04-30T00:21:00Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the CBI Molecules being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst in the [http://robertsgroup.ecs.umass.edu/ Roberts Research Group] and on display at the [http://www.molecularplayground.org Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Human_insulin2/1&#039;&amp;gt;Insulin Dimer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is made up of two pieces called the A- and B-chain, shown above in blue and green respectively.  These two chains are joined by disulfide bonds, which are shown in yellow.  This single piece made up of the A- and B-chains is the active form of the insulin hormone.  This is the form that binds the insulin receptor on fat or muscle cells in the body, singling them to take up glucose, or sugar, from the blood and save it for later.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/2insulin_dimers/2&#039;&amp;gt;Two Insulin Dimers&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is able to pair-up with itself and form a dimer by forming hydrogen bonds between the ends of two B-chains.  Then, 3 dimers can come together in the presence of zinc ions and form a hexamer.  Insulin is stored in the hexameric form in the body.       &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_hexamer/2&#039;&amp;gt;Symmetric Insulin Hexamer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is a hormone that controls sugar metabolism and storage in the human body.  The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.  Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes.  The image below highlights the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7.  It is believed that the hydrophobic sections on the B-chain cause insulin aggregation which initially caused problems in the manufacture and storage of insulin for pharmaceutical use.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_ph7/1&#039;&amp;gt;Insulin: pH 7&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081902</id>
		<title>User:Whitney Stoppel/sandbox1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081902"/>
		<updated>2010-04-30T00:19:32Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the CBI Molecules being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst in the [http://robertsgroup.ecs.umass.edu/ Roberts Research Group] and on display at the [http://www.molecularplayground.org Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Human_insulin2/1&#039;&amp;gt;TextToBeDisplayed&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is made up of two pieces called the A- and B-chain, shown above in blue and green respectively.  These two chains are joined by two disulfide bonds.  This single piece made up of the A- and B-chains is the active form of the insulin hormone.  This is the form that binds the insulin receptor on fat or muscle cells in the body, singling them to take up glucose, or sugar, from the blood and save it for later.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/2insulin_dimers/2&#039;&amp;gt;Two Insulin Dimers&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is able to pair-up with itself and form a dimer by forming hydrogen bonds between the ends of two B-chains.  Then, 3 dimers can come together in the presence of zinc ions and form a hexamer.  Insulin is stored in the hexameric form in the body.       &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_hexamer/2&#039;&amp;gt;Symmetric Insulin Hexamer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is a hormone that controls sugar metabolism and storage in the human body.  The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.  Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes.  The image below highlights the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7.  It is believed that the hydrophobic sections on the B-chain cause insulin aggregation which initially caused problems in the manufacture and storage of insulin for pharmaceutical use.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_ph7/1&#039;&amp;gt;Insulin: pH 7&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081899</id>
		<title>User:Whitney Stoppel/sandbox1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081899"/>
		<updated>2010-04-30T00:07:07Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the CBI Molecules being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst in the [http://robertsgroup.ecs.umass.edu/ Roberts Research Group] and on display at the [http://www.molecularplayground.org Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
Insulin is made up of two pieces called the A- and B-chain.  These two chains are joined by two disulfide bonds.  This single piece made up of the A- and B-chains is the active form of the insulin hormone.  This is the form that binds the insulin receptor on fat or muscle cells in the body, singling them to take up glucose, or sugar, from the blood and save it for later.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/2insulin_dimers/1&#039;&amp;gt;Two Insulin Dimers&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is able to pair-up with itself and form a dimer by forming hydrogen bonds between the ends of two B-chains.  Then, 3 dimers can come together in the presence of zinc ions and form a hexamer.  Insulin is stored in the hexameric form in the body.       &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_hexamer/2&#039;&amp;gt;Symmetric Insulin Hexamer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is a hormone that controls sugar metabolism and storage in the human body.  The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.  Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes.  The image below highlights the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7.  It is believed that the hydrophobic sections on the B-chain cause insulin aggregation which initially caused problems in the manufacture and storage of insulin for pharmaceutical use.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_ph7/1&#039;&amp;gt;Insulin: pH 7&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081898</id>
		<title>User:Whitney Stoppel/sandbox1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081898"/>
		<updated>2010-04-30T00:05:38Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the CBI Molecules being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
Insulin is made up of two pieces called the A- and B-chain.  These two chains are joined by two disulfide bonds.  This single piece made up of the A- and B-chains is the active form of the insulin hormone.  This is the form that binds the insulin receptor on fat or muscle cells in the body, singling them to take up glucose, or sugar, from the blood and save it for later.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/2insulin_dimers/1&#039;&amp;gt;Two Insulin Dimers&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is able to pair-up with itself and form a dimer by forming hydrogen bonds between the ends of two B-chains.  Then, 3 dimers can come together in the presence of zinc ions and form a hexamer.  Insulin is stored in the hexameric form in the body.       &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_hexamer/2&#039;&amp;gt;Symmetric Insulin Hexamer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is a hormone that controls sugar metabolism and storage in the human body.  The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.  Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes.  The image below highlights the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7.  It is believed that the hydrophobic sections on the B-chain cause insulin aggregation which initially caused problems in the manufacture and storage of insulin for pharmaceutical use.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_ph7/1&#039;&amp;gt;Insulin: pH 7&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081897</id>
		<title>User:Whitney Stoppel/sandbox1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081897"/>
		<updated>2010-04-30T00:01:02Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;&#039;Insulin&#039;&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
Insulin is made up of two pieces called the A- and B-chain.  These two chains are joined by two disulfide bonds.  This single piece made up of the A- and B-chains is the active form of the insulin hormone.  This is the form that binds the insulin receptor on fat or muscle cells in the body, singling them to take up glucose, or sugar, from the blood and save it for later.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/2insulin_dimers/1&#039;&amp;gt;Two Insulin Dimers&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is able to pair-up with itself and form a dimer by forming hydrogen bonds between the ends of two B-chains.  Then, 3 dimers can come together in the presence of zinc ions and form a hexamer.  Insulin is stored in the hexameric form in the body.       &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_hexamer/2&#039;&amp;gt;Symmetric Insulin Hexamer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is a hormone that controls sugar metabolism and storage in the human body.  The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.  Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes.  The image below highlights the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7.  It is believed that the hydrophobic sections on the B-chain cause insulin aggregation which initially caused problems in the manufacture and storage of insulin for pharmaceutical use.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_ph7/1&#039;&amp;gt;Insulin: pH 7&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081896</id>
		<title>User:Whitney Stoppel/sandbox1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081896"/>
		<updated>2010-04-29T23:50:19Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;&#039;Insulin&#039;&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
Insulin is made up of two pieces called the A- and B-chain.  These two chains are joined by two disulfide bonds.  This single piece made up of the A- and B-chains is the active form of the insulin hormone.  This is the form that binds the insulin receptor on fat or muscle cells in the body, singling them to take up glucose, or sugar, from the blood and save it for later.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Insulin is able to pair-up with itself and form a dimer by forming hydrogen bonds between the ends of two B-chains.  Then, 3 dimers can come together in the presence of zinc ions and form a hexamer.  Insulin is stored in the hexameric form in the body.       &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_hexamer/2&#039;&amp;gt;Symmetric Insulin Hexamer&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Insulin is a hormone that controls sugar metabolism and storage in the human body.  The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.  Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes.  The image below highlights the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7.  It is believed that the hydrophobic sections on the B-chain cause insulin aggregation which initially caused problems in the manufacture and storage of insulin for pharmaceutical use.&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_ph7/1&#039;&amp;gt;Insulin: pH 7&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081892</id>
		<title>User:Whitney Stoppel/sandbox1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081892"/>
		<updated>2010-04-29T23:41:15Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;&#039;Insulin&#039;&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
Insulin is a hormone that controls sugar metabolism and storage in the human body.  The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.  Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes.  The hydrophobic portions of the insulin monomer lead to aggregation over time in hydrophilic solutions, initially causing problems in the manufacture and storage for pharmaceutical use.&lt;br /&gt;
&lt;br /&gt;
Insulin is made up of two pieces called the A- and B-chain.  These two chains are joined by two disulfide bonds.  This single piece made up of the A- and B-chains is the active form of the insulin hormone.  This is the form that binds the insulin receptor on fat or muscle cells in the body, singling them to take up glucose, or sugar, from the blood and save it for later.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Insulin is able to pair-up with itself and form a dimer by forming hydrogen bonds between the ends of two B-chains.  Then, 3 dimers can come together in the presence of zinc ions and form a hexamer.  Insulin is stored in the hexameric form in the body.       &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Insulin_hexamer/2&#039;&amp;gt;Symmetric Insulin Hexamer&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081582</id>
		<title>User:Whitney Stoppel/sandbox1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081582"/>
		<updated>2010-04-28T18:29:13Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;&#039;Insulin&#039;&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
Insulin is a hormone that controls sugar metabolism and storage in the human body.  The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.  Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes.  The hydrophobic portions of the insulin monomer lead to aggregation over time in hydrophilic solutions, initially causing problems in the manufacture and storage for pharmaceutical use.&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081581</id>
		<title>User:Whitney Stoppel/sandbox1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081581"/>
		<updated>2010-04-28T18:23:57Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;&#039;Insulin&#039;&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
Insulin is a hormone that controls sugar metabolism and storage in the human body.  The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.  Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes.  The hydrophobic portions of the insulin monomer lead to aggregation over time in hydrophilic solutions, initially causing problems in the manufacture and storage for pharmaceutical use.  &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Human_insulin/1&#039;&amp;gt;Insulin dimer synthesized in E. coli&amp;lt;/scene&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Human_insulin/2&#039;&amp;gt;Hydrophobic (gray) and polar (purple) portions of the insulin dimer&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081580</id>
		<title>User:Whitney Stoppel/sandbox1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081580"/>
		<updated>2010-04-28T18:23:37Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;&#039;Insulin&#039;&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
Insulin is a hormone that controls sugar metabolism and storage in the human body.  The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.  Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes.  The hydrophobic portions of the insulin monomer lead to aggregation over time in hydrophilic solutions, initially causing problems in the manufacture and storage for pharmaceutical use.  &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Human_insulin/1&#039;&amp;gt;Insulin dimer synthesized in E. coli&amp;lt;/scene&amp;gt;&amp;lt;/n&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Human_insulin/2&#039;&amp;gt;Hydrophobic (gray) and polar (purple) portions of the insulin dimer&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081579</id>
		<title>User:Whitney Stoppel/sandbox1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081579"/>
		<updated>2010-04-28T18:23:04Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;math&amp;gt;Insert formula here&amp;lt;/math&amp;gt;&#039;&#039;&#039;Insulin&#039;&#039;&#039;&amp;lt;/n&amp;gt;&lt;br /&gt;
Insulin is a hormone that controls sugar metabolism and storage in the human body.  The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.  Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes.  The hydrophobic portions of the insulin monomer lead to aggregation over time in hydrophilic solutions, initially causing problems in the manufacture and storage for pharmaceutical use.  &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Human_insulin/1&#039;&amp;gt;Insulin dimer synthesized in E. coli&amp;lt;/scene&amp;gt;&amp;lt;/n&amp;gt;&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Human_insulin/2&#039;&amp;gt;Hydrophobic (gray) and polar (purple) portions of the insulin dimer&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081578</id>
		<title>User:Whitney Stoppel/sandbox1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081578"/>
		<updated>2010-04-28T18:21:32Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;&#039;Insulin&#039;&#039;&#039;&lt;br /&gt;
Insulin is a hormone that controls sugar metabolism and storage in the human body.  The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.  Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes.  The hydrophobic portions of the insulin monomer lead to aggregation over time in hydrophilic solutions, initially causing problems in the manufacture and storage for pharmaceutical use.  &lt;br /&gt;
&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Human_insulin/1&#039;&amp;gt;Insulin dimer synthesized in E. coli&amp;lt;/scene&amp;gt;&lt;br /&gt;
&amp;lt;scene name=&#039;User:Whitney_Stoppel/sandbox1/Human_insulin/2&#039;&amp;gt;Hydrophobic (gray) and polar (purple) portions of the insulin dimer&amp;lt;/scene&amp;gt;&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=File:HumanInsulin.pdb&amp;diff=1081560</id>
		<title>File:HumanInsulin.pdb</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=File:HumanInsulin.pdb&amp;diff=1081560"/>
		<updated>2010-04-28T17:28:45Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: uploaded a new version of &amp;quot;Image:HumanInsulin.pdb&amp;quot;&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Human Insulin&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=File:HumanInsulin.pdb&amp;diff=1081557</id>
		<title>File:HumanInsulin.pdb</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=File:HumanInsulin.pdb&amp;diff=1081557"/>
		<updated>2010-04-28T17:24:03Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: uploaded a new version of &amp;quot;Image:HumanInsulin.pdb&amp;quot;: Human Insulin&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Human Insulin&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=File:HumanInsulin.pdb&amp;diff=1081555</id>
		<title>File:HumanInsulin.pdb</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=File:HumanInsulin.pdb&amp;diff=1081555"/>
		<updated>2010-04-28T17:21:46Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: Human Insulin&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Human Insulin&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081553</id>
		<title>User:Whitney Stoppel/sandbox1</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=User:Whitney_Stoppel/sandbox1&amp;diff=1081553"/>
		<updated>2010-04-28T17:19:15Z</updated>

		<summary type="html">&lt;p&gt;Whitney Stoppel: New page: &amp;#039;&amp;#039;&amp;#039;Insulin&amp;#039;&amp;#039;&amp;#039;&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;&#039;Insulin&#039;&#039;&#039;&lt;/div&gt;</summary>
		<author><name>Whitney Stoppel</name></author>
	</entry>
</feed>