How many water molecules would be needed to break a protein with 200 peptide bonds into its monomer subunits? What types of reaction would this be?

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Answer:

The correct answer would be - 200 water molecules.

Explanation:

Peptide bonds present in the dipeptide or polypeptide easily break into its monomer which is amino acids by the process known as hydrolysis or more specifically amide hydrolysis. In this process, the water molecule is added to the protein where the peptide bond is broken down into its constituents.

If a polypeptide or protein has 200 peptide bonds that required 200 water molecules to break all the bonds into its monomer substituents as the number of peptide bonds required a number of a water molecule to break down.

200 water molecules would be needed.

Peptide bonds instead in dipeptides and polypeptides readily break down into their monomers, which would be amino acids, through a procedure termed hydrolysis, and maybe more particularly amide hydrolysis.

  • The water molecule becomes joined to the protein throughout that step, as well as the peptide bond would be broken down itself into the elements.
  • Whether a polypeptide, as well as protein, comprises 200 peptide bonds, it takes 200 water to break down just about all the connections breakdown in and out of monomer linkers, where the number of peptide bonds needed a no. of molecules (water) to break down.

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