From Proteopedia

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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 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.