From Proteopedia

Trypsin

Trypsin is a serine protease that is produced in the pancreas. Serine protease means that it is an enzyme that cleaves amino acid sequences and that a serine residue is located in the active site of the enzyme. In order to prevent it from breaking down the proteins in the pancreas of the organism that produces it, it is first produced as the inactive zymogen, proenzyme trypsinogen.

Structural Aspects

Trypsin is an enzyme that is composed of one, sequence unique, chain consisting of 58 amino acid residues. Looking at the of trypsin one can see it is composed of two alpha helices(pink) and two beta sheets(yellow).

Observing the of trypsin one can easily follow the primary sequence of the amino acids as it begins at the amide or N-terminal end(dark blue), and progresses to the carboxyl or C-terminal end with the final 58th amino acid reside (red).

Trypsin is also held together by three located between the 5 and 55, 14 and 38, and 30 and 51 Cystine residues(yellow).

To determine the polar and non-polar sections of an enzyme, the various R groups coming of of the are analyzed. Looking at the , the side chains can be classified as either non-polar otherwise known as hydrophobic (literally meaning water fearing) or polar otherwise known as hydrophilic (water loving). Looking first at the you can easily see the classifications of the nonpolar(pink) and polar(yellow) side chains. Looking at this molecule you can see the majority of the yellow strands are found near the exterior of the enzyme where they would act with the polar enviroment, while many of the nonpolar residues are hidden inside. Looking at the model you can achieve a better grasp on the organization of these nonpolar and polar sections of the enzyme. Polar regions again appear in yellow, nonpolar pink, and some of the waters that would interact with the enzyme appear gray in the diagram.

Function