5a) Draw this peptide at the physiological pH (7.4) with the following 1-letter codes: F-R-I-D-A-Y b) What is its net overall charge?
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- 1. A pentapeptide has the sequence of H2N-Glu-His-Leu-Arg-Gly-COOH. a) What is the net charge of the peptide at pH 3, 8, and 11? (Use pka values for side chains and terminal amino and carboxyl groups in the table provided.) peptide. b) Estimate the pl for this pK, values Abbreviation/ symbol pk, M, (-COOH) (-NH5) (R group) pK; pKR Hydropathy Occurrence in index* proteins (%)* Amino acid pl Nonpolar, aliphatic R groups Glycine Alanine Proline Valine 2.34 -0.4 Gly G Ala A Pro P 75 9.60 5.97 7.2 89 115 2.34 9.69 10.96 6.01 6.48 5.97 1.8 1.6 4.2 3.8 4.5 7.8 5.2 1.99 117 131 Val V 2.32 2.36 9.62 9.60 6.6 9.1 Leucine Leu L 5.98 Isoleucine lle I 131 2.36 2.28 9.68 6.02 5.3 Methionine Met M 149 9.21 5.74 1.9 2.3 Aromatic R groups Phenylalanine Tyrosine Tryptophan 2.8 -1.3 3.9 3.2 Phe F 165 1.83 9.13 9.11 9.39 5.48 2.20 Tyr Y Trp W 181 10.07 5.66 204 2.38 5.89 -0.9 1.4 Polar, uncharged R groups Serine Ser S 105 2.21 6.8 9.15 9.62 5.68 5.87 5.07 5.41 5.65 -0.8 Threonine Thr T 119 2.11 -0.7 5.9…4) a) Draw the peptide ASYTL at pH 7 and 12. b) Draw a Titration Curve for this peptide. c) If this protein were separated by isoelectric focusing, at what pH would you expect to find it? d) Alcohols usually don't behave as a weak acids, but tyrosine does. Explain why Y ionizes, while S and T do not. e) Is Y ionization physiologically relevant? Explain. f) Y is capable of being phosphorylated by kinases in vivo. What mutation might you introduce to render Y unphosphorylatable? Constitutively phosphorylated?You have isolated the following peptide: His-Ser-Arg-Ala-Glu-Leu-Pro-Gly A) Calculate the approximate charge of this peptide at pH 1, pH 3, pH 5, pH8, pH 11, and pH 14. B) What is the PI of this peptide?
- Consider the following peptide: Lys-Tyr-Glu-His-Arg-Ala-Asp-Arg-Glu-Tyr-Lys a) What is the net charge of this peptide at pH=1? Show your work. b) What is the net charge of this peptide at pH=14? Show your work.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?Consider a short peptide with the sequence M-C-Q-L-Y-P-E-D-K. List the ionizable groups in this peptide, and the net charge of the whole peptide at pH a) 1.5, b) 7.0, and c)12.0.
- 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.Given the peptide Lys-Glu-Trp a) Draw the appropriate titration curve for this peptide. Label X and Y axis b) On the graph use X to mark point at which peptide have 0 net charge and Y to mark point where peptide have positive 1 net chargeGiven the following Peptide: Q6 *H;N-Phe-Asp-Ala-Arg-Gy-His-Arg-Asp-Glu-His-Tyr-CO 6a. What is the peptide's net charge at pH 2.0, pH 6.0, pH 7.4, and pH 10.2? (show work) 6b. What is the approximate isoelectric point of this peptide?
- The sequence of a 29 aa long peptide can be determined from the following data. a) Treatment of the peptide with dansyl chloride reveals that the amino terminal is Val. b) Trypsin digestion, separation of peptides and Edman degradation give sequences for peptide fragments as follows: Val-Gly-Ala-His-Ala-Gly-Glu-Tyr-Gly-Ala-Glu-Ala-Thr-Glu Ala-Ala-Trp-Gly-Lys Val-Leu-Ser-Pro-Ala-Lys Thr-Asn-Val-Lys c) Chymotrypsin digestion, separation of peptides, and Edman degradation give the following sequences for fragments: Gly-Ala-Glu-Ala-Thr-Glu Gly-Lys-Val-Gly-Ala-His-Ala-Gly-Glu-Tyr Val-Leu-Ser-Pro-Ala-Lys-Thr-Asn-Val-Lys-Ala-Ala-Trp What is the sequence for the peptide?1) Indicate the total charge of the peptide at pH 7.0, 9.0, and 11.0 2) Determine the isoelectric point (pI) for this peptide. Show the relevant pKa’s and your calculation. 3) What is the fraction of the peptide that has the N-terminal amino group deprotonated at pH 9.In your laboratory, you plan to use ion exchange chromatography to separate the peptide show below from a mixture of different peptides at pH 7.0. Peptide: GDVRWKKFQR A) Draw the structure of the peptide shown above at pH 7. B) Determine the charge of the peptide at pH 7. C) Should you choose a matrix containing DEAE(anion exchange) or CM (cation exchange)? Explain your reasoning in 3-5 sentences. SUBMIT A SINGLE DOCUMENT (PDF) WITH THE THREE REQUIRED ANSWERS. Upload Choose a File