Porcine dynorphin is a neuropeptide having 17 amino acid residues. Its structure is shownbelow.Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln8. How does trypsin catalyze the hydrolysis of peptides? You can answer this question byidentifying the amino acids involved and whether the hydrolysis is at their amino side or thecarboxyl side or if particular amino acids end up at the N-teminal end or at the C-terminalend.9. List down the different fragments that would result if dynorphin were cleaved by trypsin.10. How does chymotrypsin catalyze the hydrolysis of peptides? You can answer this questionby identifying the amino acids involved and whether the hydrolysis is at their amino side orthe carboxyl side or if particular amino acids end up at the N-teminal end or at the C-terminal end.11. List down the different fragments that would result if dynorphin were cleaved bychymotrypsin.12. Cyanogen bromide is a chemical reagent which also cleaves peptide bonds. What is/are thesite(s) of cleavage of cyanogen bromide?13. List down the different fragments that would result if dynorphin were cleaved by cyanogenbromide.14. List down the different fragments that would result if dynorphin were treated withmyoglobin.15. List down the different fragments that would result if dynorphin were treated withhemoglobin.

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Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter10: From Proteins To Phenotypes

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Problem 14QP: If phenylalanine was not an essential amino acid, would diet therapy (the elimination of...

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If phenylalanine was not an essential amino acid, would diet therapy (the elimination of phenylalanine from the diet) for PKU work?
Porcine dynorphin is a neuropeptide having 17 amino acid residues. Its structure is shown below. Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln How does trypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C-terminal end. List down the different fragments that would result if dynorphin were cleaved by trypsin. . How does chymotrypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C- terminal end. List down the different fragments that would result if dynorphin were cleaved by chymotrypsin. . Cyanogen bromide is a chemical reagent which also cleaves peptide bonds. What is/are…
The melanocyte-stimulating hormone a-melanotropin has the following sequence: Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val In the one-letter code of amino acids, this sequence would be: SYSMEHFRWGKPV STSMGHFAWGKPV O SYSMDHFAWGKPV O SYSMEHFAWGLPV
After the polypeptide shown below was treated with maleic anhydride, it was hydrolyzed by trypsin. (After a polypeptide is treated with maleic anhydride, trypsin will cleave the polypeptide only on the C-side of arginine.) Gly-Ala-Asp-Ala-Leu-Pro-Gly-Ile-Leu-Val-Arg-Asp-Val-Gly-Lys-Val-Glu-Val-Phe-Glu-Ala-Gly-Arg-Ala-Glu-Phe-Lys-Glu-Pro-Arg-Leu-Val-Met-Lys-Val-Glu-Gly-Arg-Pro-Val-Gly-Ala-Gly-Leu-Trp In what order will the fragments be eluted from an anion-exchange column using a buffer of pH = 5?
H CH₂ H₂C HC-CH3 CH₂ H H₂C (S) H₂C H CH₂ CH₂ CH₂ NH O C NH NH₂ a) Which of the following statements about this peptide are correct? Group of answer choices Treatment of this peptide with trypsin generates two products. This peptide is a substrate for carboxypeptidase A Treatment of this peptide with cyanogen bromide generates a pentapeptide and a tripeptide. Treatment of this peptide with chymotrypsin generates three products. Treatment of this peptide with elastase generates 2 products. None of the above statements are correct. b) What is the sequence of this peptide using one letter abbreviations? c) What is the pH which would correspond to the ionization of the peptide as drawn above? 1, 5, 7, 10, 14
Draw a peptide for cys-asn- pro-gly (Using the same format in picture)
V-M-Y-F-E-N: This is the single-letter amino acid abbreviation for a peptide. What is the net charge of this peptide at pH 7.0? An enzyme called a protein tyrosine kinase can attach phosphates to the hydroxyl groups of tyrosine (Y). What is the net charge of the peptide at pH 7.0 after it has been phosphorylated by a tyrosine kinase? What is the likely source of phosphate used by the kinase for this reaction?
An oligopeptide has the following amino acid sequence: NH2-Ala-Glu–Leu–Trp–Tyr-Ser–Gly–Lys–Leu-Ala–Arg-Ala-Phe-Ile-Pro–Gly-COOH a) Estimate the net electric charge of the molecule at pH 8.0 and pH 11.0. b) If the above peptide is passed through a cation exchange chromatographic column (that is, the matrix of the column has negative charges) stabilized at pH 8.0, would you expect it to be retained on the column? c) Indicates the number of fragments, and the sequence of each of them, that would be obtained when treating the peptide in question with: i) trypsin, ii) chymotrypsin.
Consider the following peptide: Lys-His-Asp-Glu-Phe-Cys-Ala-Asp-His-Arg What is the net charge of this peptide at pH = 1? What is the net charge of this peptide at pH = 14?
The melanocyte-stimulating peptide hormone α-melanotropin has the following sequence: Ser–Tyr–Ser–Met–Glu–His–Phe–Arg–Trp–Gly–Lys–Pro–Val(a) Write the sequence using the one-letter abbreviations.(b) Calculate the molecular weight of α-melanotropin, using data in as shown.
The melanocyte-stimulating peptide hormone a-melanotropin has the following sequence: Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val (a) Write the sequence using the one-letter abbreviations. (b) Calculate the molecular weight of a-melanotropin, a da'
Draw the structure of the peptide: Val-His-Leu-Thr-Pro-Val-Glu-Lys-Ser-Ala-Val-Thr What is the significance of the peptide described?

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