Molecular Playground/Trypsin
From Proteopedia
(Difference between revisions)
| (5 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| + | <applet size='[450,338]' frame='true' align='right' | ||
| + | caption='Trypsin catalytic site' /> | ||
| + | |||
| + | |||
| + | <scene name='Molecular_Playground/Trypsin/Trypsin/5'>Trypsin</scene> | ||
| + | |||
| + | |||
| + | |||
| + | |||
==Trypsin== | ==Trypsin== | ||
| - | Trypsin is a serine protease that is used as a tool to aid in protein identification by cleaving the protein on the c-terminal of Lysine and arginine residues resulting in peptides with lower molecular weights. | + | Trypsin is a serine protease that is used as a tool to aid in protein |
| + | identification by cleaving the protein on the c-terminal of Lysine and | ||
| + | arginine residues resulting in peptides with lower molecular weights. | ||
| - | <applet size='[450,338]' frame='true' align='right' | ||
| - | caption='YYY' /> | ||
| - | + | Banner: Scene shows the catalytic site where trypsin cleaves amide bonds | |
Current revision
|
Trypsin
Trypsin is a serine protease that is used as a tool to aid in protein identification by cleaving the protein on the c-terminal of Lysine and arginine residues resulting in peptides with lower molecular weights.
Banner: Scene shows the catalytic site where trypsin cleaves amide bonds
