The digestive enzyme chymotrypsin is a serine protease which cleaves peptide bonds near large, hydrophobic residues. Chymotrypsin is also important for activating a number of other digestive enzymes. This study addresses the energetics of the reaction mechanism of chymotrypsin using the bovine gamma-chymotrypsin protein structure (PDB ID 1AFQ) using the PM7 Hamiltonian as implemented in MOPAC2012. The lowest energy conformation of enzyme bound to substrate was found to have a number of important salt bridges that stabilize the structure. After finding the lowest energy conformation, the energy profile for the steps in the accepted mechanism was investigated. A greater understanding of the reaction energetics of chymotrypsin is of interest because there are a number of serine proteases in humans, including elastase, which is implicated in emphysema, and thrombin, which plays a role in some clotting disorders.

Modeling some features of the reaction mechanism of chymotrypsin using semiempirical methods

249th National Meeting (2015)

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