Through acid hydrolysis for 24 hours, Jackson obtained the following amino aci residues: Ala-Arg-Cys-Gln-Lys-Phe-Tyr-Val No phenylthiohydantoin structure was obtained after Edman analysis. Furthermore, no C-terminal residue was also obtained after treatment with carboxypeptidase. He then used trypsin and chymotrypsin enzymes as cleaving agents. Trypsin cleaves at the C-terminal of basic amino acids Lys and Arg while chymotrypsin cleaves at the C-terminal of aromatic amino acids such as Phe, Tyr, and Trp. The results of trypsin and chymotrypsin cleavage were listed in the table below: Enzyme Amino Acid Residues Chymotrypsin Trypsin Determine the sequence of the polypeptide using the one-letter code of the amin acids. Kindly check the lecture slide for the amino acid one-letter codes. Drag th correct boxes to their respective markers. The directionality of the N-to-C terminals is also specified below. N-terminal Val-Lys-Ala-Phe + Gln-Arg-Cys-Tyr Cys-Tyr-Val-Lys + Ala-Phe-Gln-Arg I KA|SR|YP|LF|C|T V C-terminal 1

Through acid hydrolysis for 24 hours, Jackson obtained the following amino aci residues: Ala-Arg-Cys-Gln-Lys-Phe-Tyr-Val No phenylthiohydantoin structure was obtained after Edman analysis. Furthermore, no C-terminal residue was also obtained after treatment with carboxypeptidase. He then used trypsin and chymotrypsin enzymes as cleaving agents. Trypsin cleaves at the C-terminal of basic amino acids Lys and Arg while chymotrypsin cleaves at the C-terminal of aromatic amino acids such as Phe, Tyr, and Trp. The results of trypsin and chymotrypsin cleavage were listed in the table below: Enzyme Amino Acid Residues Chymotrypsin Trypsin Determine the sequence of the polypeptide using the one-letter code of the amin acids. Kindly check the lecture slide for the amino acid one-letter codes. Drag th correct boxes to their respective markers. The directionality of the N-to-C terminals is also specified below. N-terminal Val-Lys-Ala-Phe + Gln-Arg-Cys-Tyr Cys-Tyr-Val-Lys + Ala-Phe-Gln-Arg I KA|SR|YP|LF|C|T V C-terminal 1

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 54AP

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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.
Somatostatin is a tetradecapeptide of the hypothalamus that inhibits the release of pituitary growth hormone. Its amino acid sequence has been determined by a combination of Edman degradations and enzymic hydrolysis experiments. On the basis of the following data, deduce the primary structure of somatostatin: 1. Edman degradation gave PTH-Ala. 2. Selective hydrolysis gave peptides having the following indicated sequences: Phe-Trp Thr-Ser-Cys Lys-Thr-Phe Thr-Phe-Thr-Ser-Cys Asn-Phe-Phe-Trp-Lys Ala-Gly-Cys-Lys-Asn-Phe 3. Somatostatin has a disulfide bridge.
Determine the amino acid sequence of a polypeptide from the following data:Acid-catalyzed hydrolysis gives Ala, Arg, His, 2 Lys, Leu, 2 Met, Pro, 2 Ser, Thr, and Val.Carboxypeptidase A releases Val.Edman’s reagent releases PTH-Leu.Treatment with cyanogen bromide gives three peptides with the following amino acid compositions:1. His, Lys, Met, Pro, Ser 2. Thr, Val 3. Ala, Arg, Leu, Lys, Met, Ser
Determine the amino acid sequence of a polypeptide from the following data: Acid-catalyzed hydrolysis gives Ala, Arg, His, 2 Lys, Leu, 2 Met, Pro, 2 Ser, Thr, and Val. Carboxypeptidase A releases Val. Edman’s reagent releases PTH-Leu. Treatment with cyanogen bromide gives three peptides with the following amino acid compositions: 1. His, Lys, Met, Pro, Ser 2. Thr, Val 3. Ala, Arg, Leu, Lys, Met, Ser Trypsin-catalyzed hydrolysis gives three peptides and a single amino acid: 1. Arg, Leu, Ser 2. Met, Pro, Ser, Thr, Val 3. Lys 4. Ala, His, Lys, Met
Using the information below, determine the amino acid sequence of the peptide, and explain how your structure is consistent with each piece of information. Complete hydrolysis by 6 M HCl at 110°C followed by amino acid analysis indicated the presence of Gly, Leu, Phe, and Tyr in a 2:1:1:1 molar ratio. Treatment of the peptide with1-fluoro-2,4-dinitrobenzene followed by complete hydrolysis and chromatography indicated the presence of the 2,4-dinitrophenyl derivative of tyrosine. No free tyrosine could be found. Complete digestion of he peptide with pepsin (which cleaves on the amino side of aromatic residues) followed by chromatography yielded a dipeptide containing Phe and Leu and a tripeptide containing Tyr and Gly in a 1:2 ratio.
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
Bradykinin is a linear nonapeptide released by blood plasma globulin in response to a wasp sting. It is a very potent pain-causing agent. Its constituent amino acids are 2R, G, 2F, 3P, S. The sue of 2,4-dinitrofluorobenzene and carboxypeptidase shows that both terminal residues are arginine. Partial hydrolysis of bradykinin gives the following di- and tripeptides: FS + PGF +PP + SPF + FR + RP
Show the peptides that would result from cleavage by the indicated reagent: Val-Arg-Gly-Met-Arg-Ala-Ser by carboxypeptidase A
The Arg-Gly-Asp tripeptide (RGD) is a well-known tumour targeting peptidemotif. Explain how you would synthesise H-Arg-Gly-Asp-OH, starting fromthe constituent amino acids? Explain all steps that are necessary and discuss amechanism for one side chain protection and one C terminus protection.
Chemistry Given TETRAPEPTIDE: Prolinyl-Argininyl-Cysteinyl-Tryptophan Predict the direction of the peptide in electrophoresis at pH 7 and pH11.5. (Use table on the upper right for the estimated pK values of some functional groups).
Given the following peptide SEPIMAPVEYPK(a) Estimate the net charge at pH 7 and at pH 12. Assume the pKa valuesgiven in as shown. (b) How many peptides would result if this peptide were treated with(1) cyanogen bromide, (2) trypsin, or (3) chymotrypsin?(c) Suggest a method for separating the peptides produced by chymotrypsintreatment.
Show the peptides that would result from cleavage by the indicated reagent: Arg-Ser-Pro-Lys-Lys-Ser-Glu-Gly by trypsin