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Suggest a reasonable strategy for the synthesis of the dipeptide Leu-Phe, using established protocol for peptide synthesis.
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- Write the complete structures for the following peptides. Tell whether each peptide is acidic, basic, or neutral.(a) methionylthreonine (b) threonylmethionineDraw out the peptide IYV and clearly label/identify all the Phi, Psi, and peptide bonds present in the peptide. Be sure to draw out the entire peptide and label the N- and C-termini. Which type of secondary structure would this peptide most likely take on (assuming it would take on a secondary structure)?.Outline the steps needed to synthesize the tetrapeptide Ala–Leu–Ile–Gly using the Merrifield technique.
- What reaction conditions are needed to achieve complete peptide hydrolysis to its amino acid components? Draw a curly arrow mechanism for hydrolysis of a peptide bond under these conditions.Deduce the sequence of a pentapeptide that contains the amino acids Ala, Glu, Gly, Ser, and Tyr, from the following experimental data. Edman degradation cleaves Gly from the pentapeptide, and carboxypeptidase forms Ala and a tetrapeptide. Treatment of the pentapeptide with chymotrypsin forms a dipeptide and a tripeptide. Partial hydrolysis forms Gly, Ser, and the tripeptide Tyr–Glu–Ala.Show the mechanism and explain how the Ala-Val-Ile peptide bond is formed.
- With reference to the following peptide: (a) Identify the N-terminal and Cterminal amino acids. (b) Name the peptide using one-letter abbreviations. (c) Label all the amide bonds in the peptide backbone.(a) Draw a structural formula for the products formed when alanine is treated with the following reagents. (i) (Boc)20, NaOH (ii) CbzCI, NazCO3 (iii) 2-Methylpropene, p-TSOH (b) Enfuvirtide, a 36-amino-acid peptide drug, was manufactured at a multi-tonne per year scale. The manufacture relied on solid phase synthesis with Barlos resin as the solid support. Part of the solid phase synthesis is shown below. Write the structure of the product A and discuss the cleavage mechaniśm of the peptide from the resin. 1. Fmoc-Leu-OH, DIPEA 2. 20% piperidine in DMF 3. Fmoc-Glu('Bu)-OH, HBTU, HOBt 4. 20% piperidine in DMF 5. Fmoc-Leu-OH, HBTU, HOBT 6. 20% piperidine in DMF 7. Fmoc-Leu-OH, HBTU, HOBE 8. 20% piperidine in DMF 9. 10% HOAC in CH2CI2 Barlos resinCleavage of the following peptide with cyanogen bromide would result in the production of smaller peptides, whereas cleavage with trypsin would result in the production of Ala-Lys-Met-Glu-Asp-Cys-Ile-Phe-Met-Cys-Trp-Glu three, three one, two two, two three, two
- Draw the complete structures of the following peptides:(a) Thr-Phe-Met (b) serylarginylglycylphenylalanine (c) IMQDK (d) ELVISPropose a synthesis for the peptide leu-lys-cysDeduce 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.