1. A pentapeptide has the sequence of H2N-Glu-His-Leu-Arg-Gly-COOH. a) What is the netcharge of the peptide at pH 3, 8, and 11? (Use pka values for side chains and terminalamino and carboxyl groups in the table provided.)peptide.b) Estimate the pl for thispK, valuesAbbreviation/symbolpk,M, (-COOH) (-NH5) (R group)pK;pKRHydropathy Occurrence inindex* proteins (%)*Amino acidplNonpolar, aliphaticR groupsGlycineAlanineProlineValine2.34-0.4Gly GAla APro P759.605.977.2891152.349.6910.966.016.485.971.81.64.23.84.57.85.21.99117131Val V2.322.369.629.606.69.1LeucineLeu L5.98Isoleucinelle I1312.362.289.686.025.3MethionineMet M1499.215.741.92.3Aromatic R groupsPhenylalanineTyrosineTryptophan2.8-1.33.93.2Phe F1651.839.139.119.395.482.20Tyr YTrp W18110.075.662042.385.89-0.91.4Polar, unchargedR groupsSerineSer S1052.216.89.159.625.685.875.075.415.65-0.8ThreonineThr T1192.11-0.75.91.9CysteineAsparagineGlutamineCys CAsn N1211321461.962.022.1710.288.182.54.34.28.80-3.5Gin Q9.13-3.5Positively chargedR groupsLysineHistidineArginineLys KHis HArg R9.74-3.9-3.21462.188.9510.535.91551.829.176.007.592.31742.179.0412.4810.76-4.55.1Negatively chargedR groupsAspartateGlutamateAsp DGlu E1331472.773.221.885.39.609.673.654.25-3.52.19-3.56.3

Amino acids are organic compounds which is compose of amine group, carboxylate group, hydrogen and…

Answered: A pentapeptide has the sequence of…

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter9: Gene Expression And Gene Regulation

Section: Chapter Questions

Problem 15QP

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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.
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? c) Show resonance structures for the protonated version of Arginine's side chain.
For the peptide Ala-Cys-His-Ile-Leu-Asp a. Write the single letter code for the amino acid residues b. What is the charge of the peptide at pH 7.0. Assign the following pKa values: 3,4,6,8,9 c. What is the pI of the peptide
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?
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?
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 charge
Consider the peptides Pro-Gin-Val-Phe-His-Asp-Cys and His-Gln-Pro-Cys-Asp-Phe-Val. How do these two peptides differ? (Select all that apply.) The two peptides have different compositions. The two peptides have different isoelectric points. The two peptides have different titration curves. The two peptides differ in amino acid sequence. [References] If you were to have a mythical amino acid based on glutamic acid, but one in which the hydrogen that is attached to the y-carbon were replaced by another amino group, what would be the predominant form of this amino acid at pH 12 if the pK, value were 10 for the unique amino group? (Select all that apply.) Both of the carboxyl groups are deprotonated. The amino acid-carries a negative 2 charge. The amino acid carries a negative 4 charge. The amino groups are in the form -NH". Both of the amino groups are deprotonated.
a. An oligopeptide ALVGALGATPTPQMWSHSWRGVSIKS was digested with trypsin.Which method would be most appropriate for separating the products: ion exchange or gel filtration chromatography? Explain.b. Suppose that the peptide was digested with cyanogen bromide. What would be the optimal separation technique? Explain
Predict the fragments that will be generated from the treatment of the following peptide with: a) trypsin; b) chymotrypsin; c) and S. aureus V8 protease: Gly-Ala-Trp-Arg-Asp-Ala-Lys-Glu-Phe-Gly-Gln
Given 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?
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?
Calculate the pI for the following peptide: Phe-Lys-Glu-Asp-Lys-Ser-Ala (note: there is only one alpha carboxyl at the C terminus and one alpha amino group at the N terminus and don't forget to take into account the ionizable side chain groups)

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