Sandbox 30: Difference between revisions

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(Specifically PDB: 1QLQ)

==~~Structure~~ Quick Links==

==Overview and Quick Links==

Trypsin was first isolated by , Wilhelm Kühnein 1867Trypsin is a serine protease synthesized in the pancreas but is not activated until the zymogen form of trypsin is activated. This presents trypsin from digesting actual body tissue<ref> [http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6TGT-49S6WV8-1&_user=4187488&_coverDate=12/31/2003&_rdoc=1&_fmt=high&_orig=search&_origin=search&_sort=d&_docanchor=&view=c&_acct=C000062504&_version=1&_urlVersion=0&_userid=4187488&md5=a7d7e1b154a43b709d5228c4852e5d10&searchtype=a doi:10.1016/j.theochem.2003.08.072]</ref>.

An easy way to distinguish between main structural components of the protein is to view it using <scene name='Sandbox_30/Trypsin_cartoon_rainbow/2'>rainbow coloration.</scene> To see various other specific structures of Trypsin, click on their links.

* <scene name='Sandbox_30/Trypsin_cartoon_rainbow/2'>Rainbow Coloration</scene>

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==Structure==

Trypsin's primary amino acid sequence (RPDFCLEPPYAGACRARIIRYFYNAKAGLCQTFVYGGCRAKRNNFKSAEDCLRTCGGA) <ref> ~~1qlq~~ [http://bip.weizmann.ac.il/oca-bin/send-seq?1qlq_A]</ref> forms the <scene name='Sandbox_30/Backbone/1'>backbone</scene> of the protein, which then folds into secondary structures, consisting of two <scene name='Sandbox_30/Helixs_maroon/3'>α helices</scene> and two <scene name='Sandbox_30/Sheets_green/4'>β sheets</scene>. Both of the α helices are right handed and the β sheets are anti-parallel. The order of the secondary structures is easily visible when using the <scene name='Sandbox_30/Trypsin_cartoon_rainbow/2'>rainbow coloration</scene> scheme to identify secondary structures. The N-terminus (blue) is the beginning of trypsin and the C-terminus (agua-green) is the end.

Trypsin's primary amino acid sequence (RPDFCLEPPYAGACRARIIRYFYNAKAGLCQTFVYGGCRAKRNNFKSAEDCLRTCGGA) <ref>[http://bip.weizmann.ac.il/oca-bin/send-seq?1qlq_A 1qlq]</ref> forms the <scene name='Sandbox_30/Backbone/1'>backbone</scene> of the protein, which then folds into secondary structures, consisting of two <scene name='Sandbox_30/Helixs_maroon/3'>α helices</scene> and two <scene name='Sandbox_30/Sheets_green/4'>β sheets</scene>. Both of the α helices are right handed and the β sheets are anti-parallel. The order of the secondary structures is easily visible when using the <scene name='Sandbox_30/Trypsin_cartoon_rainbow/2'>rainbow coloration</scene> scheme to identify secondary structures. The N-terminus (blue) is the beginning of trypsin and the C-terminus (agua-green) is the end.

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@@ Line 6: / Line 6: @@
 (Specifically PDB: 1QLQ)
 <applet load='1QLQ' size='450' frame='true' align='right' caption='Click on the links to the left to view different structural aspects. Ligand shown: SO4'  />
-==Structure Quick Links==
+==Overview and Quick Links==
+Trypsin was first isolated by , Wilhelm Kühnein 1867Trypsin is a serine protease synthesized in the pancreas but is not activated until the zymogen form of trypsin is activated.  This presents trypsin from digesting actual body tissue<ref> [http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6TGT-49S6WV8-1&_user=4187488&_coverDate=12/31/2003&_rdoc=1&_fmt=high&_orig=search&_origin=search&_sort=d&_docanchor=&view=c&_acct=C000062504&_version=1&_urlVersion=0&_userid=4187488&md5=a7d7e1b154a43b709d5228c4852e5d10&searchtype=a doi:10.1016/j.theochem.2003.08.072]</ref>.
 An easy way to distinguish between main structural components of the protein is to view it using <scene name='Sandbox_30/Trypsin_cartoon_rainbow/2'>rainbow coloration.</scene>  To see various other specific structures of Trypsin, click on their links.
 * <scene name='Sandbox_30/Trypsin_cartoon_rainbow/2'>Rainbow Coloration</scene>
@@ Line 22: / Line 23: @@
 ==Structure==
-Trypsin's primary amino acid sequence (RPDFCLEPPYAGACRARIIRYFYNAKAGLCQTFVYGGCRAKRNNFKSAEDCLRTCGGA) <ref> 1qlq [http://bip.weizmann.ac.il/oca-bin/send-seq?1qlq_A]</ref> forms the <scene name='Sandbox_30/Backbone/1'>backbone</scene> of the protein, which then folds into secondary structures, consisting of two <scene name='Sandbox_30/Helixs_maroon/3'>α helices</scene> and two <scene name='Sandbox_30/Sheets_green/4'>β sheets</scene>.  Both of the α helices are right handed and the β sheets are anti-parallel. The order of the secondary structures is easily visible when using the <scene name='Sandbox_30/Trypsin_cartoon_rainbow/2'>rainbow coloration</scene> scheme to identify secondary structures.  The N-terminus (blue) is the beginning of trypsin and the C-terminus (agua-green) is the end.
+Trypsin's primary amino acid sequence (RPDFCLEPPYAGACRARIIRYFYNAKAGLCQTFVYGGCRAKRNNFKSAEDCLRTCGGA) <ref>[http://bip.weizmann.ac.il/oca-bin/send-seq?1qlq_A 1qlq]</ref> forms the <scene name='Sandbox_30/Backbone/1'>backbone</scene> of the protein, which then folds into secondary structures, consisting of two <scene name='Sandbox_30/Helixs_maroon/3'>α helices</scene> and two <scene name='Sandbox_30/Sheets_green/4'>β sheets</scene>.  Both of the α helices are right handed and the β sheets are anti-parallel. The order of the secondary structures is easily visible when using the <scene name='Sandbox_30/Trypsin_cartoon_rainbow/2'>rainbow coloration</scene> scheme to identify secondary structures.  The N-terminus (blue) is the beginning of trypsin and the C-terminus (agua-green) is the end.