nsDraw the pentapeptide REACH (one letter abbreviations) in the most prevalent ionizationstate at 8.4 with the biologically preferred stereochemistry but with a cis peptide bond atA and C, Then sketch a plot showing the % of this peptide in the zwitterionic state as afunction of pH (pH 2 to pH 10)- label the isoelectric point and 2 other exact points onthe graph.

Recall that: Amino acid sequences are written with N-terminal amino acid on the left and C-terminal…

Answered: Draw the pentapeptide REACH (one letter…

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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draw the primary structure of the polypeptide at physiological pH range of 7.35-7.45 using condensed structures 3-letter abbreviations with a hyphen representing peptide bond give the name of the peptide, determine the net charge, and calculate the isoelectric point DYINWAH
Calculate the isoelectric point (pI) of the peptide structure shown. Use table 3.1 for pKa values.
The amino acid arginine ionizes according to the following scheme: (a) Calculate the isoelectric point of arginine. You can neglect contributionsfrom 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, giventhe pI you calculated in part a? Explain your answer.
A peptide has the sequence: Glu–His–Trp–Ser–Gly–Leu–Arg–Pro–Gly1. What would be the net charge of the molecule at pH a) 3, b) 8, and c) 11? (Use pKa values. Do not calculate the value per se, but instead estimate considering only fully protonated, or deprotonated states. Then estimate the pI for this peptide. Show full, clear and complete procedure
Consider a peptide with the sequence Ala-Glu-Arg-Leu. Assume the ionizable groups have the pKa values listed in Table 2.1 of your text. (a) Draw the predominant ionic form of the peptide at pH 7.4. (b) Determine the net charge of the predominant form of the peptide at pH 7.4. (c) Calculate the pI of the peptide.
A. Write the structure of the following peptide at pH 5.0 and calculate its net charge at this pH. Asp-His-Tyr-Arg-Lys-Leu-Thr-Gln. Based on the pKa value of the ionizable groups. B. A polypeptide consisting only of L-glutamate residues (poly-L-glutamate) may have a random coil or helical structure depending on pH. Explain this behavior by indicating at what pH values the helical structure will be favored.
For the following pentapeptides: Ser-Glu-Gly-His-Ala and Gly-His-Ala-Glu-Ser A. Compute their isoelectric pH (pI). Show full solution. Use standard pKa values. B. Do these peptides with the same amino acid composition have different net charges at pH 7.0? Explain briefly. C. Would you expect the titration curves of the two peptides to differ? Why or Why not?
e) What would be the predominant ionization states of this amino acid at physiological pH (7.4) and at this pH, what would the ratio of these two states be (show the calculation)?
Calculate the net charge of the following peptide at pH 2, pH 6 and pH 14 (use 2 and 9 as pKa values for the carboxylic acid and amino groups, respectively, use the attached table for the side chain pKa values). Ile-Leu-Ile-Lys-Glu-Cys-His-Glu-Met-Ile-Ser-Thr-Arg-Tyr
Given the titration curve of the hypothetical polyprotic acid X at 0.100 M concentration (pKa1=4.0, pKa2=8.0, pKa3=12.0) titrated with 0.600 M NaOH, identify the pH at point C, H, E, and M.
the enzyme LCK catalyzes the hydrolysis of the peptide KEY in 5.0 mM phosphate buffer at pH 7.0. The enzyme is known to obey Michaelis-Menten Kinetics. Under the conditions of this experiment: Vmax= 10 mmol/min/mg Km (KEY) = 0.20 mM Draw the complete structure of the tripeptide KEY and calculate its molecular weight Sketch the titration curve of the above tripeptide and label it.Determine the net charge of the peptide at each pk value Calculate the PI pf the peptide and draw the structure of the peptide at the isoelectric point.
Draw a Cys–Gly–Asn tripeptide. Identify the peptide bond and the N- and C-termini, and determine the peptide’s net charge at neutral pH.

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