Draw the structure of the PTH derivative product you would obtain by Edman degradation of the following peptides:
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Q: Draw the structure of the PTH derivative you would obtain by Edman degredation of the peptide: ALPF.
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Draw the structure of the PTH derivative product you would obtain by Edman degradation of the following peptides:
(a) I-L-P-F
(b) D-T-S-G-A
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- 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'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, 14Draw the structure of the PTH derivative you would obtain by Edman degredation of the peptide: ALPF.
- The key reaction steps in the Edman degradation of polypeptides, which removes the N-terminal amino acid in the form of a "phenylthiohydantoin" (PTH-amino acid), are shown below. What is the expected outcome if the N-terminal amino acid is proline (Pro)? (The structure of proline is provided below for your reference.) NH-C00 NH CO0 phenyl isothiocyanate PITC NH CO0 NH CO0 peptide without the thiszolinone original Nterminal amino acid HE a PTH-amino acid Proline: HN HN. O Edman's reagent will not react with an N-terminal proline.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 8. 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. 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 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. 11. List down the different fragments that would result if dynorphin were cleaved by chymotrypsin. 12. Cyanogen bromide is a chemical reagent which also cleaves peptide bonds.…A seven-residue peptide was found to have an amino acid composition including glu, val, Lys, met, leu, and trp (there is more than one copy of one amino acid). Several reactions on samples of the peptide resulted in the following: a) Trypsin has no effect on the heptapeptide. b) If one cycle of Edman degradation provides the PTH derivative shown below, what does this tell you about the oligopeptide under investigation? [image] c) Chymotrypsin treatment yields a dipeptide, a tetrapeptide, and a free amino acid. Possibilities? d) The tetrapeptide contains val, lys, and met (only). What information does this give you? e) Cyanogen bromide treatment generates a dipeptide, a tetrapeptide, and free Lys. f)What is the sequence of the peptide?
- The peptide cys-leu-glu-ala-cys-lys is at pH 7 in oxidizing conditions. Part a) Draw the peptide's titration curve. Part b) What would the pI of the peptide be around?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 endorphins are a group of naturally occurring neurotransmitters that act in a manner like morphine to control pain. Research has shown that the biologically active parts of the endorphin molecules are simple pentapeptides called enkephalins. Draw the structure of the methionine enkephalin with the sequence Tyr-Gly-Gly-Phe-Met. Identify the N-terminal and C-terminal amino acids. Bradykinin is a nonapeptide that stimulates smooth muscle contraction, dilates blood vessels, causes pain, and is a component of bee venom. Give the IUPAC name of the nonapeptide. Note: The selected photo is the sequence of Bradykinin.
- Show the peptides that would result from cleavage by the indicated reagent: a. Val-Arg-Gly-Met-Arg-Ala-Ser by carboxypeptidase A b. Ser-Phe-Lys-Met-Pro-Ser-Ala-Asp by cyanogen bromide c. Arg-Ser-Pro-Lys-Lys-Ser-Glu-Gly by trypsinThe hydrolysis of a phenylalanine-containing peptide is catalyzed by a-chymotrypsin with the following results. Calculate KM and Vmax for the reaction. What is the equation of the line?A NONAPEPTIDE that attacks and kills cancer cells has just been recently isolated from a rare fungus. Amino acid analysis of the peptide reveals the following information below: (NOTE: when the sequence is not known, a comma separates the amino acids) Hydrezine Nonapeptide Acid Hydrolysis (4 N HCI) at 110 C (2) Arg. Gin, (2) Tyr, Gly, Ser, Thr, and Met 2,4-dinitrolluorobenzene DNP-Thr Gin and Peptide 1 (Arg. Thr, Ser) modified free amino acids Cleavoge with Trypsin, then thrometography Peptide 2 (Gly, Tyr, Arg) Met Tripeptide (yenegen bromide Dipeptide Cleovoge with Chymetrypsin, then chromatography Peptide 3 (Arg, Ser, Tyr, Thr) Amino acid Peptide 4 (Gly, Arg, Tyr) When answering the questions below, please use the one-letter code for the amino acid, with NO spaces and symbols between each letter. 1. What is the N-terminal AA residue? 2. What is the C-terminal AA residue? 3. What is the sequence of Peptide 1? 4. What is the sequence of Peptide 4? 5. What is the overall amino acid…