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Sandbox 49

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Revision as of 00:46, 30 October 2010 by Student (Talk | contribs)
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Please do NOT make changes to this Sandbox. Sandboxes 30-60 are reserved for use by Biochemistry 410 & 412 at Messiah College taught by Dr. Hannah Tims during Fall 2012 and Spring 2013.

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Trypsin

Trypsin is a serine protease that is produced in the pancreas as the inactive proenzyme trysinogen. It hydrolyses proteins (peptide bonds) and it is found in many vertebrates. Trypsin cleaves peptide chains mainly at the (red) side of the amino acids lysine or arginine, except when either is followed by proline. The German physiologist Wilhelm Kühne (1837-1900) discovered trypsin in 1876.

Structure

This is the of trypsin. The of trypsin is highlighted in blue and its are highlighted in green. The , also known as the main chain of trypsin. The of trypsin can be seen with purple representing polar areas and gray representing nonpolar areas.The of trypsin with red showing the negative charges (anionic) and blue showing the positively charged areas(cationic), while purple shows the uncharged areas. surrounding trypsin.N to C can be seen beginning at the blue N 5' terminal to the red C 3' terminal. contact with molecule. contact with different , including oxygen(red), sodium (blue) and sulfur (yellow).

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