Sandbox 14
From Proteopedia
(Difference between revisions)
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<applet load="1gzx" size="300" color="white" frame="true" align="right" caption="Trypsin" scene='Sandbox_14/Bovine_trypsin/5' /> | <applet load="1gzx" size="300" color="white" frame="true" align="right" caption="Trypsin" scene='Sandbox_14/Bovine_trypsin/5' /> | ||
| - | Trypsin is a serine protease responsible for the breakdown of hydrolysis of proteins. This process is biologically applicable in the process of digestion. | + | Trypsin is a serine protease responsible for the breakdown of hydrolysis of proteins. This process is biologically applicable in the process of digestion. Trypsin like all other serine proteases is very specific in its reaction. It cleaves at peptide bonds after positive residues. These are arginine and lysine. The active site of trypsin is composed of a catalytic triad-Hs57,Asp102 and Cys 195. Each of these groups have a specific role to play in the hydrolysis of peptide bonds. |
| - | Trypsin acts at | ||
| - | .. | ||
<scene name='Sandbox_14/Trypsin/1'>TextToBeDisplayed</scene> | <scene name='Sandbox_14/Trypsin/1'>TextToBeDisplayed</scene> | ||
Revision as of 16:57, 22 June 2010
Please do NOT make changes to this sandbox. Sandboxes 10-30 are currently reserved by Prof. Sheila Jaswal at Amherst College.
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Trypsin is a serine protease responsible for the breakdown of hydrolysis of proteins. This process is biologically applicable in the process of digestion. Trypsin like all other serine proteases is very specific in its reaction. It cleaves at peptide bonds after positive residues. These are arginine and lysine. The active site of trypsin is composed of a catalytic triad-Hs57,Asp102 and Cys 195. Each of these groups have a specific role to play in the hydrolysis of peptide bonds.
