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- 1, on derivative curves, there are several sharp peaks. what points in the ionisation of the amino acid do these peaks represent? 2. what is the relationship between equivalence points and the PKA of each ionisable groupsGiven the following peptideSEPIMAPVEYPK(a) Estimate the net charge at pH 7 and at pH 12. Assume the pKa valuesgiven in Table (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.1a. suggest a test you will use to show that a given food substance contains protein. b. show how you will use i. modified Gabriels synthesis ii. Streckers synthesis to prepare phenylalanine in the laboratory. 2a. Describe in details how you will determine the primary structure of protein. b. You have been given a mixture of lysine, histidine and cysteine. The isoelectric point of the amino acids are as follows, Histidine 7.64 Lysine 9.74 Cysteine 5.02 Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components. 3a. A decapeptide has the following amino acid composition, Ala2, Arg, Cys, Glu, Gly, Leu, Lys, Phe, Val Partial hydrolysis yields the following tripeptides, Cys-Glu-Leu +Gly-Arg-Ala +Lys-Val-Phe-Gly Reaction of the decapeptide with 2,4-dinitrofluorobenzene yields 2,4-dinitrophenylsine. From the experimental data, deduce the primary structure of the…
- Write out the steps needed to synthesize the following peptide using the Merrifield method.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.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.
- Consider the Blosum-62 matrix in Figure 6.9. Replacement of which three amino acids never yields a positive score? What features of these residues might contribute to this observation?Consider the partial sequence of a peptide.I L W A N R M S H V L F A V E ASelect all amino acid residues likely to be on the solvent‑exposed surface once the peptide folds into its native conformation.In the case of serine, threonine and tyrosine they have the -OH group in their residue. I'm wondering even though all of them has the -OH groups in their residue. but only the tyrosine has the pKa value with the -OH grouup.
- 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.1.Show how you will usei.Modified Gabriel’s Synthsis to prepare phenylalanine in the laboratory.ii. Streckers’s Synthesis to prepare phenylalanine in the laboratory. 2. You have been given a mixture of lysine, histidine and cysteine. The isoelectric point of the amino acids are as follows:Histidine 7.64Lysine 9.74Cystenie 5.02Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.4b) Canavanine is closely related to arginine, and like arginine its side group has a +1 charge when protonated. If you dissolved canavanine in an aqueous solution at pH 10, what would the net charge on a molecule of canavanine be? Please show your work or make it clear how you determined the charge contribution from each ionizable group.
