Sandbox 46: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
<applet load='1QLQ' size='300' frame='true' align='right' caption='Trypsin' /> | <applet load='1QLQ' size='300' frame='true' align='right' caption='Trypsin' /> | ||
=Trypsin= | =Trypsin= | ||
Trypsin, a member of the serine protease family, is produced in the pancreas and found in the digestive tracks of vertebrates. To avoid pancreatic self-degradation, trypsin is synthesized as trypsinogen, a zymogen. Cleavage by enteropeptidase allows tryspin to enter its active form. As a serine protease, trypsin contains a serine residue in its active site. | Trypsin, a member of the serine protease family, is produced in the pancreas and found in the digestive tracks of vertebrates. To avoid pancreatic self-degradation, trypsin is synthesized as trypsinogen, a zymogen. Cleavage by enteropeptidase allows tryspin to enter its active form. As a serine protease, trypsin contains a serine residue in its active site. | ||
==Structure== | ==Structure== | ||
| Line 16: | Line 16: | ||
<scene name='Sandbox_46/Polar_vs_nonpolar_wire/1'>Wire</scene> | <scene name='Sandbox_46/Polar_vs_nonpolar_wire/1'>Wire</scene> | ||
==Stability== | |||
<scene name='Sandbox_46/Disulfide_bonds/3'>Disulfide</scene> | <scene name='Sandbox_46/Disulfide_bonds/3'>Disulfide</scene> | ||
<scene name='Sandbox_46/Disulfide_bonds_123/1'>DS bonds labeled</scene> | <scene name='Sandbox_46/Disulfide_bonds_123/1'>DS bonds labeled</scene> | ||
<scene name='Sandbox_46/Hbonds_backbone/1'>H bonds backbone</scene> | |||
<scene name='Sandbox_46/H_bonds_r_groups/1'>H bonds r groups</scene> | |||
==Function== | |||
<scene name='Sandbox_46/Ac1/1'>Active Site 1</scene> | <scene name='Sandbox_46/Ac1/1'>Active Site 1</scene> | ||
| Line 30: | Line 37: | ||
<scene name='Sandbox_46/Ac_all/1'>All active sites</scene> '''Shared active site''' | <scene name='Sandbox_46/Ac_all/1'>All active sites</scene> '''Shared active site''' | ||
Revision as of 01:54, 29 October 2010
|
Trypsin
Trypsin, a member of the serine protease family, is produced in the pancreas and found in the digestive tracks of vertebrates. To avoid pancreatic self-degradation, trypsin is synthesized as trypsinogen, a zymogen. Cleavage by enteropeptidase allows tryspin to enter its active form. As a serine protease, trypsin contains a serine residue in its active site.
Structure
To follow the primary structure (amino acid sequence) of Trypsin, click here. The N-terminus is blue and the C-terminus is red.
The secondary structure of Trypsin consists of two alpha helices (light green) and two beta sheets (peach). The yellow and red molecules are not part of the Trypsin structure; they were added during crystallization to freeze Trypsin in a specific conformation. Fix THIS. they bind at active site
Stability
Function
All active sites Shared active site
