Lotem haleva/test page: Difference between revisions

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Lotem Haleva, Michal Harel

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-==Your Heading Here (maybe something like 'Structure')==
+==Trypsin==
-<StructureSection load='1y3v' size='340' side='right' caption='Trysine' scene=''>
+<StructureSection load='1y3v' size='340' side='right' caption='Bovine trypsine complex with inhibitor and Ca+2 ion (green) (PDB code [[1y3v]])' scene=''>
-This is a default text for your page '''Lotem haleva/test page'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
+'''Trypsin''' is a serine protease that found in the digestive system of many vertebrates, where it hydrolyses proteins<ref>doi:10.1016/0076-6879(94)44004-2</ref>.
+Trypsin is produced in the pancreas as the inactive zymogen protease called trypsinogen. trypsinogen secreted into the small intestine where it activates trypsinogen into trypsin by the enzyme Antrookinaz using proteolytic decomposition.
-is a serine protease, found in the digestive system of many vertebrates, where it hydrolyses proteins<ref>doi:10.1016/0076-6879(94)44004-2</ref>.
+Trypsin Break peptide chains at the carboxyl side of the amino acids lysine or arginine,
-Trypsin is produced in the pancreas as the inactive protease trypsinogen.
+except when it is followed by proline. .
-Trypsin Break peptide chains mainly at the carboxyl side of the amino acids lysine or arginine,
-except when either is followed by proline. It is used for numerous biotechnological processes.
-The process is commonly referred to as trypsin proteolysis or trypsinisation,
-and proteins that have been digested/treated with trypsin are said to have been trypsinized.
 == Function ==
-In the duodenum, trypsin catalyzes the hydrolysis of peptide bonds, breaking down proteins into smaller peptides.
+Trypsin catalyzes the hydrolysis of peptide bonds and cutting proteins into smaller peptides in the duodenum.
-The enzymatic mechanism is similar to that of other serine proteases. These enzymes contain a catalytic triad consisting of <scene name='60/607865/Active_site/2'>histidine-57, aspartate-102, and serine-195</scene>. These three residues form a charge relay that serves to make the active site serine nucleophilic.
+== Structure and Mechanism ==
+Trypsin  is a medium size globular protein that contains either <scene name='60/607865/Helix/1'>alpha helix</scene> and <scene name='60/607865/Sheets/1'>beta sheets</scene>.
+The enzymatic mechanism of Trypsin is similar to the other serine proteases. These enzymes contain a catalytic triad consisting of <scene name='60/607865/Active_site/2'>histidine-57, aspartate-102, and serine-195</scene>, These three residues makes the active site serine nucleophilic <ref>doi:10.1007/s00018-005-5160-x</ref>.
 Trypsin contains an "oxyanion hole" formed by the backbone amide hydrogen atoms of <scene name='60/607865/Oxyanion_hole/1'>Gly-193 and Ser-195</scene> , which serves to stabilize the developing negative charge on the carbonyl oxygen atom of the cleaved amides.
-The  <scene name='60/607865/Asp_189/1'>aspartate residue</scene>  located in the catalytic pocket (S1) of trypsin is responsible for attracting and stabilizing positively charged lysine and/or arginine, and is, thus, responsible for the specificity of the enzyme.
+The  <scene name='60/607865/Asp_189/1'>aspartate residue</scene>  located in the catalytic pocket of trypsin is responsible for attracting and stabilizing positively charged lysine or arginine, and as a result responsible for the specificity of the enzyme <ref> doi:10.1021/pr0705035</ref>.
-== Mechanism ==
-== Relevance ==
 == Structural highlights ==
+There are different ways to present the protein structure :<scene name='60/607865/Balls_and_stik/1'>balls and stick</scene>, <scene name='60/607865/Surface/1'>surface</scene> and <scene name='60/607865/Backbone/1'>Backbone</scene>. Another way to view the protein is <scene name='60/607865/Rainbow_n_to_c/1'>Rainbow</scene> that show the protein from the N (blue) to C terminal (green).
-This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
 </StructureSection>
 == References ==
 <references/>