00:01
Hello everyone, in this question we have been asked that the acid hydrolysis of nonpeptide gave the amino acid composition that is lysine, arginine, alanine, glycine, ferrene, threonine, methionine, and phenylalanine.
00:27
So here the sequence of the non -a peptide after the acid cleavage will be alanine, arginine, ferrene, phenylalanine, lysine, and glycine because lysine here are present two times, methionine, threonine, and glycine.
00:49
So acid cleaves the peptide into its constituent amino acid and thus we now have the 9 amino acid that is present in the non -a peptide.
01:02
Then here the next question says that carboxypeptidease a treatment release the glycine.
01:09
So carboxypeptidase a cleaves the peptide bond at the c terminal residue and here glycine is released after treatment and hence there we can tell that glycine is present at c terminal residue of the peptide.
01:25
Then we have been said that trypsin cleaves at the basic residue.
01:31
So trypsin cleaves at the glycine and arginine and pepsin cleaves at phenylalanine and the cnbr cleaves at the methionine...