What Does Edman Degradation Reveal About Peptide Sequence?

AI Thread Summary
The discussion revolves around determining the structure of an unknown pentapeptide E based on its amino acid composition and the results of Edman degradation and carboxypeptidase treatment. The peptide consists of glycine, tryptophan, proline, valine, and alanine, with proline being released first by carboxypeptidase. Edman degradation yielded three derivatives, indicating the sequence of amino acids, with tryptophan, glycine, and valine appearing in that order. Clarifications are sought regarding the specific type of carboxypeptidase used and the meaning of "separate Edman degradations." The conversation highlights the importance of understanding enzymatic specificity in peptide sequencing.
chem_monkey
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I'm looking at a (uni) past paper and it has one of those typical Qs - a molecular weight determination has shown that an unknown peptide E is a pentapeptide and that it contains the amino acids glycine, tryptophan, proline, valine and alanine. Treatment of pentapeptide E with carboxypeptidase gives proline as the first free amino acid released. Separate Edman degradations provided the following derivatives: and it shows three compounds, with the first containing tryptophan, second just glycine, third valine.
Based upon this analysis, draw the structure of the original pentapeptide and explain how you have arrived at this structure. Show mechanistic detail where appropriate (15 marks).

Anyone know?
 
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Which flavor of Carboxypeptidase are you using? "Separate Edman degradations..." refers to what?
 
chemisttree said:
Which flavor of Carboxypeptidase are you using? "Separate Edman degradations..." refers to what?

what flavor?
 
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