Pls explain the steps on why it came to be because I have a hard understanding this lesson T - T You have isolated from a rare fungus an octapeptide that prevents baldness and you wish to determine its amino acid sequence. The amino acid composition is K2, D, Y, F, G, S. A. Reaction of the intact peptide with dansyl chloride yields dansyl - A. Cleavage with trypsin yields peptides whose compositions are: (K, A, S) and (G, F, K) plus a dipeptide. Reaction with chymotrypsin releases free D, a tetrapeptide with composition (k, S, F. A) and a tripeptide whose composition following acid hydrolysis is (G, K, Y). The enzymatic digests are each carried out on the whole, undansylated peptide. What is the sequence?

Pls explain the steps on why it came to be because I have a hard understanding this lesson T - T You have isolated from a rare fungus an octapeptide that prevents baldness and you wish to determine its amino acid sequence. The amino acid composition is K2, D, Y, F, G, S. A. Reaction of the intact peptide with dansyl chloride yields dansyl - A. Cleavage with trypsin yields peptides whose compositions are: (K, A, S) and (G, F, K) plus a dipeptide. Reaction with chymotrypsin releases free D, a tetrapeptide with composition (k, S, F. A) and a tripeptide whose composition following acid hydrolysis is (G, K, Y). The enzymatic digests are each carried out on the whole, undansylated peptide. What is the sequence?

Organic Chemistry

9th Edition

ISBN:9781305080485

Author:John E. McMurry

Publisher:John E. McMurry

Chapter26: Biomolecules: Amino Acids, Peptides, And Proteins

Section26.SE: Something Extra

Problem 28MP

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Similar questions

An unknown decapeptide was isolated and characterized. Complete hydrolysis of this peptide gave : F(2), A,G,C,K,N,T, W and V. Treatment with carboxypeptidase releases A. Reaction with Edman’s reagent gave PTH-T and a nonapeptide. The nonapeptide was treated with trypsin and gave 2 peptides: (V-C-G-A) and (N-FF-W-K). Give the sequence of amino acid in the decapeptide.
Determine the primary structure of an octapeptide from the following data: Acid-catalyzed hydrolysis gives 2 Arg, Leu, Lys, Met, Phe, Ser, and Tyr. Carboxypeptidase A releases Ser. Edman’s reagent releases Leu. Treatment with cyanogen bromide forms two peptides with the following amino acid compositions: 1. Arg, Phe, Ser 2. Arg, Leu, Lys, Met, Tyr Trypsin-catalyzed hydrolysis forms the following two amino acids and two peptides: 1. Arg 2. Ser 3. Arg, Met, Phe 4. Leu, Lys, Tyr
Give detailed Solution with explanation needed
Treatment of a new protein with dansyl chloride reveals two (2) dansyl-labelled derivatives of amino acids, alanine and methionine. What can you deduce about the structure of the proteinfrom these results?
Predict the products P and Q formed when the following peptide is treated with the given reagient. HS. H₂N (b) (c) (d) HS P P OH H₂N. PhNCS DIPEA H₂N. X DH P + Q OH CH
Write out the steps needed to synthesize the following peptide using the Merrifield method.
In a variation of the Merrifield solid-phase peptide synthesis, the amino group is protected by a fluorenylmethoxycarbonyl (FMOC) group. This protecting group is removed by treatment with a weak base such as the secondary amine piperidine. Write a balanced equation and propose a mechanism for this deprotection.
give detailed solution with explanation needed
pls solve this problem with in 1 hour. Explain it also. I will give multiple upvote.
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Pls help ASAP on both questions I HUMBLY REQUEST