Scientist promote catalysis. The aspartate and histidine are bound

Scientist John Northrop crystallized many enzymes and proteins in the
early twentieth century. One important enzyme he crystallized was chymotrypsin.

In the following years after his crystallization, other scientists contributed
to the characterization of this enzyme, and now, it is one of the most well
understood proteases. 

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Chymotrypsin is a digestive enzyme produced by the pancreas, and it is
responsible for the breakdown of proteins and polypeptides. Without it, proper
food digestion can not occur. Chymotrypsin consists of two chains, and is made
up of 245 amino acids (Figure 1). 

The catalytic triad is an
important component of chymotrypsin. This triad consists of residues Serine 195,
Histidine 57, and Aspartate 102 (Figure 2). Together, they work to stabilize
the enzyme and promote catalysis. The aspartate and histidine are bound to each
other by hydrogen bonds, allowing histidine to work as a base for serine.

Serine can then become a nucleophile to catalyze the breakdown of proteins.