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…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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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.
The following are structural diagrams of a selection of newly discovered amino acids. OH -の-CHs NH HO C-OH NH, AN-CH CH2 CH2 OH Ho NH, C=0 a) Select 1 amino acid. Redraw it. Label the alpha carbon and circle/highlight the entire backbone of the amino acid. b) The amino acids are part of a channel protein embedded in the cell membrane. Choose 2 amino acids (from above) that you would expect to find within the interior/middle of the cell membrane. Draw the formation of the dipeptide using the 2 amino acids you selected. Identify the other products formed in the reaction.
A) Can you please tell me which of these A.A have a negative side chain? Names of choices in picture provided. B) Can you please tell me which A.A have a hydrophobic side chain and why? Names and choices in picture provided. Thank You so much!!
Among these amino acid combinations listed above, only the combination of Lys and Glu have side chains with groups that have the greatest ability to stabilize the tertiary structure of a protein. Explain by drawing (a) why Lys and Glu side chain interaction stabilizes the tertiary structure of a protein (b) why the pairs of Glu and Asp & Arg and Pro cannot provide the stability to the protein structure.
Based on the following image, what is the N-terminal AA residue, C-terminal AA residue? What is also the sequence of peptide 2 and peptide 3? Also identify the overall amino acid sequence
At which pH would the peptide with the amino acid sequence 'KEYHR' be found in an IPG (Immobilized pH gradient) strip after successful isoelectric focusing. Show calculation. lonizable groups Alpha amine group of K Side chain group of K Side chain group of E Side chain group of Y Side chain group of H Side chain group of R Alpha carboxylic acid group of R pka 8.95 10.53 4.25 10.07 6 12.48 2.17
The amino acid arginine ionizes according to the following scheme: (a) Calculate the isoelectric point of arginine. You can neglect contributions from form I. Why? (b) Calculate the average charge on arginine when pH = 9.20. (c) Is the value of average charge you calculated in part b reasonable, given the pI you calculated in part a? Explain your answer
you have the following peptide Arg-Ile-Pro-Leu-Asp-Lys-Glu The net charge on this peptide at pH 7.0 is ?. The net charge on this peptide at 1M HCl is ?.
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.
There is parts A-D for the picture provided. A) A peptide has the sequence, Arg-Cys-His-Tyr-Glu-Asn-Lys-Asp. What is the net charge at pH 1? Choices: -5 -4 -3 -2 -1 0 +1 +2 +3 +4 +5 B) A peptide has the sequence Arg-Cys-His-Tyr-Glu-Asn-Lys-Asp. What is the net charge at pH 5? Choices: -5 -4 -3 -2 -1 0 +1 +2 +3 +4 +5 C) Same Peptide sequence, What is the net charge at pH8.5, (N-terminus is pronated) Choices: -5 -4 -3 -2 -1 0 +1 +2 +3 +4 +5 D) A peptide has the sequence, Arg-Cys-His-Tyr-Glu-Asn-Lys-Asp. What is the net charge at pH 13? Choices: -5 -4 -3 -2 -1 0 +1 +2 +3 +4 +5 Thank You!
Proline is one of the amino acids in the "special" groups of sidechains. One reason for this is the dramatic impact it can have on secondary structure. a) draw the lewis structure for a tripeptide with the sequence Ala-Pro-Ala b) Proline residues are rarely found in alpha helices - in fact, they are often referred to as helix-disrupting amino acids. Thinking about intermolecular interactions, provide an explanation for why proline might disrupt alpha-helices. c) Proline also has a similar effect on beta-sheets, and is rarely found in the middle of beta sheets. Thinking about noncovalent interactions, provide an explanation for why proline might disrupt beta-sheets.
Determine the sequence of the following 10-mer of ferritin using the data below. i. Complete acid hydrolysis of the 10-mer results in identification of 1A, 1D, 1E, 1F, 1H, 1K, 2L, 1T, 1Y ii. Digestion of the 10-mer with chymotrypsin results in 3 fragments containing (D, H, K, T), (F, L) and (A, E, L, Y) iii. Digestion of the 10-mer with V8 protease, which cuts on the C-side of acidic amino acids, results in three fragments containing (D, F, L, Y), (A, E, L) and (H, K, T) iv. Digestion with trypsin results in a fragment H-T and a fragment with all the other amino acids v. Treatment of the 10-mer with FDNB followed by complete acid hydrolysis results in the following two derivatives, DNP-1 and DNP-2 vi. Treatment of the 10-mer with a carboxypeptidase results in a free threonine

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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