Sandbox 49
From Proteopedia
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==Intermolecular Forces== | ==Intermolecular Forces== | ||
<scene name='Sandbox_49/H20/1'>Water</scene> surrounding trypsin.contact with <scene name='Sandbox_49/Dna/1'>DNA</scene> molecule. | <scene name='Sandbox_49/H20/1'>Water</scene> surrounding trypsin.contact with <scene name='Sandbox_49/Dna/1'>DNA</scene> molecule. | ||
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| - | [[Image:Image:Image_Trypsin.jpg | thumb]] | ||
Revision as of 02:18, 30 October 2010
| 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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Contents |
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. N to C can be seen beginning at the blue N 5' terminal to the red C 3' terminal.
Polarity
The of trypsin can be seen with purple representing polar areas and gray representing nonpolar areas.
Molecular Attractions
The of trypsin with red showing the negative charges (anionic) and blue showing the positively charged areas(cationic), while purple shows the uncharged areas. contact with different , including oxygen(red), sodium (blue) and sulfur (yellow).
Intermolecular Forces
surrounding trypsin.contact with molecule.
