Sandbox 30: Difference between revisions
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==Overview and Quick Links== | ==Overview and Quick Links== | ||
Trypsin was first isolated by Wilhelm Kühne in 1867<ref>[https://www.doria.fi/bitstream/handle/10024/2142/trypsinr.pdf?sequence=1 ISBN 952-10-1863-1]</ref>. Trypsin is a serine protease synthesized in the pancreas but is not activated until the zymogen form of trypsin is activated. This | Trypsin was first isolated by Wilhelm Kühne in 1867<ref>[https://www.doria.fi/bitstream/handle/10024/2142/trypsinr.pdf?sequence=1 ISBN 952-10-1863-1]</ref>. Trypsin is a serine protease synthesized in the pancreas but is not activated until the zymogen form of trypsin is activated. This prevents 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>. Serine proteases were instrumental in the discovery and subsequent study of enzymes due to there high stability and large quantities in digestive juices. One of the first proteins to be studied via X-ray crystallography was Chymotrypsin. Trypsin cleaves on the C-terminus side of lysine and arginine<ref>[http://www.pdb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb46_1.html Protein Data Bank]</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> | 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> | ||
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<scene name='Sandbox_30/A_helix_hydrogen_bonds/2'>the addition of hydrogen bonding to water molecules</scene> (water is dark blue). | <scene name='Sandbox_30/A_helix_hydrogen_bonds/2'>the addition of hydrogen bonding to water molecules</scene> (water is dark blue). | ||
The <scene name='Sandbox_30/Beta_sheet_interactions/1'>β sheets</scene> (β sheets are ball and stick) have a more bilaterally divided type of bonding. One side of the β sheets are exposed to water (pink), and are stabilized by hydrogen bonding. Additionally, there are many hydrophobic interactions (gray) on the internal side of the β sheets. There are some intramolecular hydrogen bonding which is shown as light blue(oxygen) and blue(nitrogen). | The <scene name='Sandbox_30/Beta_sheet_interactions/1'>β sheets</scene> (β sheets are ball and stick) have a more bilaterally divided type of bonding. One side of the β sheets are exposed to water (pink), and are stabilized by hydrogen bonding. Additionally, there are many hydrophobic interactions (gray) on the internal side of the β sheets. There are some intramolecular hydrogen bonding which is shown as light blue(oxygen) and blue(nitrogen). | ||
[[Image:SO4_Ligand.JPG|right|200px]] | |||
====Ligands==== | ====Ligands==== | ||
There are four <scene name='Sandbox_30/So4_ligands/1'>ligands</scene> present in 1QLQ, which are stabilized mostly by hydrogen bonding. For example, <scene name='Sandbox_30/So4_ligand_62_a/1'>SO4 62 A</scene> is stabilized by hydrogen bonds using the oxygens on SO4. There is a image to the | There are four <scene name='Sandbox_30/So4_ligands/1'>ligands</scene> present in 1QLQ, which are stabilized mostly by hydrogen bonding. For example, <scene name='Sandbox_30/So4_ligand_62_a/1'>SO4 62 A</scene> is stabilized by hydrogen bonds using the oxygens on SO4. There is a image to the right showing the bonding interaction. | ||
===Other Relevant information=== | |||
==References== | ==References== | ||
<references /> | <references /> | ||
