7. A peptide has the sequence Cys-His-Glu-Met-lle-Ser-Thra. Write out the single letter sequence of this peptide.b. What is the overall charge of the peptide? Is it acidic? Basic?c. Draw the chemical structure of the peptide at pH 7.0 and show any chargedgroupsd. What is the classification of each amino acid in this peptide regardingpolarity and charge?8. The following proteins represent a wide range of molecular weights andisoelectricpoints. Mr is the molecular weight of a single protein chain.• Protein 1: Mr 68,544; pl 6.11 (monomer)• Protein 2: Mr 29,041; pl 5.32 (dimer)Protein 3: Mr 15,805; pl 5.7 (dimer)• Protein 4: Mr 12,165; pl 4.74a. Which protein is the most acidic? Explain your answer.b. Which protein will migrate the slowest in an SDS-PAGE? Explain youranswer.c. In what order will these proteins elute from a cation exchanger at phH 8?Explain your answer.d. In what order will these proteins salt out from a pH 7 solution by thedropwise addition of saturated ammonium sulfate? Explain your answer.

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Answered: 7. A peptide has the sequence…

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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4. A particular amino acid contains a-CH,NH," group. Is this amino acid more likely to be found ce inside or the outside of the folded protein? Briefly explain. 5. The addition of ethanol, CH,CH;OH, to an aqueous solution lowers the surface tension of the solution. Predict whether adding ethanol to an aqueous protein solution will tend to stabilize or unfold the protein. Briefly explain.
1. In the separation of lysine from histidine using a sulfonated polystyrene column will it be easier to separate at pH 4 or pH 8 ? explain! 2. A peptide of the order Glx-Ala-Gly-Arg bound to a sulfonated polystyrene column at neutral pH. Is Glx Glu or Gln ? Explain !
What is the primary reason the a-helix conformation in polypeptides such a stable form? A. The a-helix structure is stabilized by hydrophobic interactions. B. The a-helix structure is stabilized by intra-helical hydrogen bonds. C. The a-helix structure is stabilized by disulfide bonds. D. The a-helix structure is stabilized by proline residues.
Draw the two amino acids serine and alanine, and a dipeptide that could be formed by combining these two amino acids (ala-ser). Draw these molecules at a pH=7. In peptide nomenclature the amino terminus is on the left and the carboxyl terminus is on the right. 1. How many waters were released by formation of this dipeptide from individual amino acids? two 2. How many hydrogen bond donors does your dipeptide have? 2 3. If you were to draw this dipeptide at a pH = 1, would the number of hydrogen bond donors change? yes, the number of H-bond
Draw the chemical structure of an alanine pentapeptide. Indicate the location of each peptide bond. Label the phi () and psi () dihedral angles. Name and briefly define the four levels of protein structure.
A-C pls
1. What is the isoelectric point (pI) of lysine which has pKa values of 2.1 for the α carboxyl group, 9.7 for the α amino group and 10.5 for the side chain amino group? 2. Which of the following is most likely to be found on the exterior of a protein? A) Pro B) Trp C) Ser D) Glu 3. The type of reaction that forms a peptide bond is A) Elimination B) Hydrolysis C) Nucleophilic substitution D) Condensation
4. Exhibit 4A The following question(s) refer to this peptide: Cys-Ala-Gly-Arg-Gln-Met Refer to Exhibit 4A. The overall, net ionic charge on this peptide at pH = 7 would be: A. +2 B. +1 C. 0 D. -1 E. -2
Calculate the isoelectric point for each amino acid.a. asparagine: pKa (COOH) = 2.02; pKa (α-NH3+) = 8.80b. methionine: pKa (COOH) = 2.28; pKa (α-NH3+) = 9.21
a. How many peptide bonds are there? b. How many amino acid residues are there? c. In exact order, identify the name of the amino acids in the peptide chain. d. Give the full name of this peptide. e. Give the 3-letter abbreviation and 1-letter abbreviation. f. Calculate the pI of this peptide.
do a and e please and For e, choose two types of interactions, and then give an example of the amino acids in this polypeptide that would interact together in that way.
A fragment of a protein commonly found in food was sequenced and found to have the sequence: RDCEHKY Draw the structure, showing the form expected to be dominant at a physiological pH (7.4). Discuss how changing the pH will affect the fragment, and what implications this has on the overall structure of the protein. What is the difference between the sequence above and the sequence YKHECDR?

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