Sandbox 50
From Proteopedia
| Line 8: | Line 8: | ||
Trypsin's primary structure is a polypeptide chain of 237 amino acids. These amino acids interact with each other mostly through hydrogen bonding to form trypsin's secondary structural units. Trypsin has many important <scene name='Sandbox_50/Secondarystructure/1'>secondary structural elements</scene>, including two alpha helices (blue), an anti-parallel beta sheet (green), and random coils (gray). The arrows on these elements point toward the carboxy terminus of the protein. These secondary structures interact together to form the fully folded, native trypsin. | Trypsin's primary structure is a polypeptide chain of 237 amino acids. These amino acids interact with each other mostly through hydrogen bonding to form trypsin's secondary structural units. Trypsin has many important <scene name='Sandbox_50/Secondarystructure/1'>secondary structural elements</scene>, including two alpha helices (blue), an anti-parallel beta sheet (green), and random coils (gray). The arrows on these elements point toward the carboxy terminus of the protein. These secondary structures interact together to form the fully folded, native trypsin. | ||
==Polar and Nonpolar Residues== | ==Polar and Nonpolar Residues== | ||
| - | Trypsin's distribution of <scene name='Sandbox_50/Nonpolarandpolar/1'>polar and nonpolar residues</scene> follow the rules of the hydrophobic effect. The | + | Trypsin's distribution of <scene name='Sandbox_50/Nonpolarandpolar/1'>polar and nonpolar residues</scene> follow the rules of the hydrophobic effect. The nonpolar (gray) residues are located on the interior of the protein so they can be shielded from water, while the polar (purple) residues are distributed on the exterior of the protein because they can interact with water. This type of residue distribution in trypsin is entropically favorable. |
Revision as of 17:58, 29 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. |
|
Trypsin
Trypsin is a medium sized, globular, digestive serine protease that is synthesized by the pancreas and secreted into the duodenum of the small intestine. Trypsin hydrolyzes peptide bonds based on side chain specificities of the amino acids surrounding the bond to be cleaved. Trypsin's specificity is for the positively charged side chains of lysine and arginine.
Structure
Trypsin's primary structure is a polypeptide chain of 237 amino acids. These amino acids interact with each other mostly through hydrogen bonding to form trypsin's secondary structural units. Trypsin has many important , including two alpha helices (blue), an anti-parallel beta sheet (green), and random coils (gray). The arrows on these elements point toward the carboxy terminus of the protein. These secondary structures interact together to form the fully folded, native trypsin.
Polar and Nonpolar Residues
Trypsin's distribution of follow the rules of the hydrophobic effect. The nonpolar (gray) residues are located on the interior of the protein so they can be shielded from water, while the polar (purple) residues are distributed on the exterior of the protein because they can interact with water. This type of residue distribution in trypsin is entropically favorable.
