You have isolated a new protease that cleaves peptide bonds on the carboxyl side of Asp and Glu. Based on the enzyme's inactivation by DIFP, you suspect that it may utilize a mechanism similar to chymotrypsin. The difference in specificity might be explained by

A.) the presence of a positively charged residue in the S1 binding pocket.

B.) the presence of a negatively charged residue in the S1 binding pocket.

C.) replacement of serine-195 with a positively charged residue.

D.)the absence of the S1 binding pocket.

The correct answer is A. the presence of a positively charged residue in the S1 binding pocket.

Explanation:

The S1 pocket is basically a deep hydrophobic pocket, which permit long uncharged amino acids like tryptophan and phenylalanine to fit inside chymotrypsin. B

Binding inside the S1 pocket, places the adjacent peptide bond at the active sites for cleavage.

it's c. elements are placed in rows based on how may valencies electrons have.

for step 7 table c on the lab "newtons law of action"   the average time it took the car to travel .25 meters   was 1.92 seconds.

the average time it took the car to travel 0.50 meters was 2.61 seconds

hope this : )