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Post by axis98b » Sun Nov 10, 2013 9:18 pm

Why don’t chymotrypsin molecules attack each other during sequencing?

It's a critical thinking question for my biochem class, that I have been trying to answer for weeks.
Any help would be appreciated.

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Post by supersapien » Mon Dec 02, 2013 9:29 am

Chymotrypsin is a digestive enzyme that cleaves proteins at specific points around the carboxy terminal ends of a large hydrophobic amino acid (like tyrosine, tryptophan, and phenylalanine). Chymotrypsin molecules can also cleave other chymotrypsin molecules but it usually doesn't happen because of the large numbers of other proteins present around chymotrypsin.

For a chymotrypsin to find another chymotrypsin is rare, hence we don't see that usually.
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