Sandbox 50

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. spinqualitylabelsall models Insert caption here Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image TrypsinTrypsin 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. StructureStructure 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 ResiduesPolar and Nonpolar Residues Trypsin's distribution of -polar and nonpolar residues- follow the rules of the hydrophobic effect. The -nonpolar- residues are located on the interior of the protein so they can be shielded from water, while the -polar- 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.