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.

2h2o2--> 2h2o + o2

this reaction is of the spontaneous decomposition of hydrogen peroxide down into water and oxygen.

add 2 molecules of hydrogen peroxide and 2 molecules of water. since oxygen is naturally diatomic, the total number of atoms of each element is now the same on both sides of the equation so it is balanced.

this may not be entirely correct but let me know.

considering the question as per the attachment

here we can see that the radon nuclide has 222 as the atomic mass number and 86 as the atomic number.

when it undergoes nuclear fission it gives polonium which has atomic mass number as 218 and atomic number will be 84 along with a helium nucleus which has 4 atomic mass number and 2 as its atomic number.

222 = 218 + 4 (atomic mass number)

86 = ? + 2; therefore ? = 86-2 = 84.

the atomic mass number of polonium will be 84.