What Can Studies Of Serine Proteases Tell Us About The Relationship Between Protein Structure, Function And Evolution?

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What can studies of serine proteases tell us about the relationship between protein structure, function and evolution?
Serine proteases are a group of important proteases which can fracture the peptide bond in the macromolecules and proteins. The serine proteases take a great part in mammal lives especially in digestion, coagulation and the complement system appears. The activation of serine proteases are all because of the change of a set of amino acid residues which includes at least one serine and that’s why the name became. Although there are about one third of the known proteolytic enzymes are serine proteases, the principle of interactions are really same: a complicate combined interaction in the catalytic triad--Ser-His-Asp. This essay will firstly talk about the mechanisms of the serine proteases and secondly mention the relationship of the protein structure, function, and evolution during the serine proteases interact. In the first part, the chymotrypsin interaction will be analyzed as an example to explain the mechanism of serine proteases interact.
Figure 1 the pymol figure of Trypsin

Figure 2 structure of the active center of chymotrypsin
Figure 3 the specific interaction of chymotrypsin
The Pymol figure shows a crystal structure of Trypsin, a typical kind of serine protease. In the middle of the Trypsin, there is a Ser-His-Asp. The mechanisms of all serine proteases including Trypsin are: firstly the serine residues in the active center are activated by

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