Interpretation:
The reactions involved in a sequential Edman degradation of MIR are to be written.
Concept introduction:
舧 Amino acids are organic compounds containing
舧 Edman degradation method is used for identification of the N-terminal amino acid in a peptideup to a maximum length of about 60 residues. In this method, phenylisothiocynate reacts with the amino group of the terminal position to form a cyclic phenylthiocarbamoyl derivative. Under acidic conditions, the terminal amino acid is cleaved from the main chain as thizolinone derivative. Thizolinone derivative is extracted to the organic solvent and it forms phenylthiohydantoin-amino acid (PTH-amino acid) derivative in the presence of acid. PTH-amino acid complex can be identified by comparison with the standard amino acids. These steps can be repeated again with the next amino acid residue in the peptide chain.
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Organic Chemistry
- (a) Redraw the tripeptide in zwitterionic form (b) Explain how ESI-MS can be used to determine which amino acid is in the middle of the sequence.arrow_forwardWhat is the name of the peptide and what is the mechanism when making it by solid phase peptide synthesis?arrow_forwardDeduce the sequence of a heptapeptide that contains the amino acids Ala, Arg, Glu, Gly, Leu, Phe, and Ser, from the following experimental data. Edman degradation cleaves Leu from the heptapeptide, and carboxypeptidase forms Glu and a hexapeptide. Treatment of the heptapeptide with chymotrypsin forms a hexapeptide and a single amino acid. Treatment of the heptapeptide with trypsin forms a pentapeptide and a dipeptide. Partial hydrolysis forms Glu, Leu, Phe, and the tripeptides Gly-Ala-Ser and Ala-Ser-Arg.arrow_forward
- Suggest a reasonable strategy for the synthesis of the dipeptide Leu-Phe, using established protocol for peptide synthesis.arrow_forwardDeduce the sequence of a heptapeptide that contains the amino acids Ala, Arg, Glu, Gly, Leu, Phe, and Ser, from the following experimental data. Edman degradation cleaves Leu from the heptapeptide, and carboxypeptidase forms Glu and a hexapeptide. Treatment of the heptapeptide with chymotrypsin forms a hexapeptide and a single amino acid. Treatment of the heptapeptide with trypsin forms a pentapeptide and a dipeptide. Partial hydrolysis forms Glu, Leu, Phe, and the tripeptides Gly–Ala–Ser and Ala–Ser–Arg.arrow_forward26) Match the following enzyme names with the process they perform. A: IHexokinasc, B: ATP Synthetase, C: Pretcase, D: Pancreatic lipase, E: RNA Polymerase, F: Dehydrogenase, G: Maltase. An enzyme that phosphorylates glucose in the glycołysis pathway. .. An enzyme that hydrolyzes peptide bonds of a large peptide into smaller active protcins. .... An enzyme that hydrolyzes triglycerides to form free fatty acids. .... An enzyme that uses Nicotinamide or Flavin coenzymes to oxidize or reduce substratcs. An enzyme that creates a complimentary piece of RNA from a DNA template.arrow_forward
- With the following amino acid side chain can the side chain of threonine form hydrogen bonds? Q.) Histidinearrow_forwardSomatostatin 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.arrow_forwardThere is a hexapeptide, and its primary structure is written down according to the following experimental results, and the analysis process is briefly written down: (1) DNP-Ala was obtained by DNFB reaction; (2) DNP-Ile was obtained by reaction with DNFB after hydrazine hydrolysis; (3) Two tripeptides were obtained by reaction with cyanogen bromide, then DNP-Leu and DNP-Ala were obtained by reaction with DNFB; (4) Fragments containing 1, 2 and 3 amino acids were obtained by trypsin hydrolysis, and the Sakakuchi reaction of the last two fragments was positive.arrow_forward
- Explain why, when the guanidino group of arginine is protonated, the double-bonded nitrogen is the nitrogen that accepts the proton.arrow_forwardPredict the effects of the following compounds on intracellular nucleosidetriphosphate levels. For each answer, plot percent initial nucleotide levelas a function of time after administration of the agent, for each of the fournucleotides (semiquantitatively). Consider not only the primary effect ofthe compound but also any indirect effects on allosteric enzymes caused bynucleotide accumulation or depletion.(a) Effect of thymidine on dNTP levels(b) Effect of trimethoprim on bacterial rNTP levels(c) Effect of fluorodeoxyuridine on dNTP levels(d) Effect of hydroxyurea on dNTP levelsarrow_forwardDraw the complete structures of the following peptides:(a) Thr-Phe-Met (b) serylarginylglycylphenylalanine (c) IMQDK (d) ELVISarrow_forward
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