Show reasoning in detail. A polypeptide was analyzed by a graduate student who w

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Show reasoning in detail.

A polypeptide was analyzed by a graduate student who was trying to determine its antibacterial properties. The following treatments produced the given results, with amino acid abbreviations separated by commas indicating the amino acids present within the given peptide fragments. Acid hydrolysis produced the following amino acids: Arg, Asx, Gly, Cys, lie. Leu, Lvs, Cys, Met, Pro, Ser, Phe One cycle of Edman degradation resulted in two PTH-derivatives: PTH-Ser and PTH-Leu The polypeptide was treated with 2-mercaptoethanol, along with a second reagent which leaves the Cys residues that were involved in disulfide bonds as charged species. This was followed by trypsin treatment and yielded the following peptide fragments: Carboxypeptidase treatment produced the following amino acid: Asp Chymotrypsin treatment yielded no peptide fragments or derivatives Pepsin treatment yielded the following peptides: lie, Dithiothreitol (DTT), a comparable substitute for 2-mercaptoethanol, followed by trypsin treatment, produced the following peptide fragments: Dithiothreitol (DTT). a comparable substitute for 2-mereaptoethanol, followed by trypsin treatment, produced the following peptide fragments: Given the above information, deduce the amino acid sequence of the peptide. Show your reasoning. When you have determined the primary structure, demonstrate and explain fully that the sequence is consistent with each experimental observation including details of your analysis through each step. Hint #1: Asx produced from the acid hydrolysis step indicates that either Asp or Asn were isolated, but the

Explanation / Answer

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1)Acid hydrolysis ( 6 N HCl + 100-1200 C for 10 -12 hrs) of the whole peptide chain into individual components
----------so the given are the types of amino acids present in the peptide chain
2) removal of NH2-derivatized amino-acids from the N-terminal to the C-terminal of a peptide chainis
--------so this step removed serine,Leu from N terminal ends
3)

4)

Carboxypeptidase A cleaves the C-terminal peptide bond of all residues except P( Pro), R(Arg), and K(Lys).
-----------so c terminal AA is arg
5)Chymotrypsin cleaves after Phe( F), Tyr(Y), and Trp(W), and also L(leu), ---carboxyl side

-------------
6) cleaves at c termianal side of Phe ,Tyr

-----so

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