From Proteopedia

proteopedia linkproteopedia link

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.

Contents 1 Trypsin 1.1 Structure 1.2 Polar vs. Nonpolar Residues 1.3 Contacts Between Structural Components and Remainder of the Protein 1.3.1 Charge

Trypsin

Trypsin is a medium size globular protein that functions as a pancreatic serine protease. Trypsin was first discovered in 1876 by Kuhne, who investigated the proteolytic activity of the enzyme.

Structure

The of the protein can be followed from N-terminus of the protein (blue) to the C-terminus of the protein (red).

Trypsin has many important structural aspects. The

spinqualitylabelsall models Trypsin protein with structural aspects shown. Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

secondary structures are shown this figure . The main backbone of the trypsin protein is shown in yellow . Trypsin has two alpha helices shown in blue and two beta sheets shown in green . The beta sheets in the Trypsin protein are antiparallel to each other and connected by a Beta-hairpin turn.

Polar vs. Nonpolar Residues

This image shows the of the residues in the protein. The polar areas of the protein are shown in pink, while the non-polar areas of the molecule are shown in light blue. The polarity of the individual amino acid residues can be seen better in the . The polar amino acid residues are again shown in pink, while the non-polar amino acid residues are shown in blue. By rotating the two representations of the polar versus non-polar areas of the protein to an aerial view, it can be seen that the polar (hydrophilic) areas are located toward the outside of the protein, while the non-polar (hydrophobic) areas are located toward the inside of the protein.

Contacts Between Structural Components and Remainder of the Protein

Charge

The charge of the different components of Trypsin are shown in this figure . The cationic (+) atoms are shown in blue, while the anionic (-) are shown in red. These charged aspects of the protein face the outside environment surrounding the protein. The light purple parts of the protein are uncharged and the gray portions of the protein are hydrophobic. These portions of the protein make up the hydrophobic core of the protein. The charged and uncharged portions of the protein directly relate to the hydrophilic and hydrophobic character of the protein.