plzzzzz help with this 31. What percent of the peptide Arg-Pro are net positively charged at pH 9.0? The table belowgives the pka's of the ionizable groups on the free amino acids.Free amino acidArginineProline1.82.0pKa of alpha-carboxyl groupA. 10%B. 30%C. 50%D. 70%E. 90%F. Need more informationpKa of alpha-aminogroup9.010.6pKa of side chain12.5none32. The ionic interactions within a protein molecule areA. Mostly contributed by the side chains of constituent amino acidsB. Determined by the contribution from the alpha-carboxyl group, alpha-amino group andside chain of every amino acid in the proteinC. Contributed by only the N-terminal and C-terminal residuesD. Independent of the amino acid composition and depend only on pH

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

Answered: 31. What percent of the peptide Arg-Pro…

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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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.
a All amino acids have at least two ionizable groups: an a-amino group (average pK₁ of 8.0) and an α-carboxylic acid group (average pK₂ of 3.1). Histidine also has an ionizable side chain (R group) with a pKa of about 6.0. One of the possible ionization states of histidine is shown in a the image. Select the pH values at which the charged form of the R group would predominate. 6.0 At what pH would the structure shown be the predominant ionization state? Consider the ionization state of all three of the functional groups. 2.2 + The protonated form of the R group of histidine is shown in the structure. The ratio of the charged (protonated) form to the deprotonated form depends on the pK₁ of the R group and the pH of the solution. 4.9 H₂N-CH-C-OH | CH₂ 11.5 + HN -NH
5. Refer to Model 2 for information relevant to this question. A sample of the peptide Lys-Glu-Ser has a net charge of zero between what two pH values? What is the pl of Lys-Glu-Ser? Model 2: The pl of a peptide is determined by examining the ionizable groups. The protonated and unprotonated forms of each ionizable group are in equilibrium. Consider the peptide Lys-Glu-Ser shown below at pH 7.2. The complete structure is on on the left and a stylized structure with just the ionizable groups is on the right. While the N-terminal is depicted as protonated, a sample of Lys-Glu-Ser is composed of a population of molecules and within that population some molecules contain a non-protonated N-terminal group at pH 7.2. may H3N* COO- H3N-CH-CIN-CH C N-CH C- H. pK 3.5 OH H. pK= 8.5 COO- CH2 CH2 CH2 NH, pK 10.0 pK 4.2 CH2 CH2 OH CH2 c=0
5 For the peptide structure in #3, (ASP-ALA-THR-LYS-GLY), use the chart at the end of this HW set to: A. Determine the net charge of the pentapeptide at pH 3, 4, 7, 10 and 11. B. Estimate the isoelectric point, pl, for this 5-amino acid peptide
4. a. Give the full names of the amino acids in this peptide. НзN — CH—С-N—CH— С-N—CH—С—О ČH3 H ČH,OH H. CH2 -ОН b. Calculate the isoelectric point (pl) of a peptide with sequence SNARE. Show your work in a table, giving the pKa values of the ionizable groups, pH, and charges. Step marks are counted. Don't need to write “protonated" or “deprotonated".
2. Consider the peptide Trp-Arg-Glu-Cys-Gly-Tyr. For the drawings requested below, please show in zig-zag style, from amino to carboxy terminus, with correct stereochemistry a. Draw the predominant form at pH = 2 b. Draw the predominant form at pH = 5 c. Draw the predominant form at pH = 7 d. Draw the predominant form at pH = 12
Bovine chymotrypsinogen has a molecular massof 25.6 kDa. Amino acid analysis shows that thisenzyme is 4.7% Gly (Mr 75.1).b. Calculate how many glycine residues are present in amolecule of bovine chymotrypsinogen
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 bioactive conformation of lead compound I was confirmed when a crystal structure was r. obtained showing I bound to its target (an enzyme). Ala-312 in His-42 Val-307 CI Asp-305 Phe-47 H. Ser-254 I bound to target protein Using the information shown above, draw the structure of an analog that you predict will exhibit improved binding to the target. Explain how you arrived at this proposed analog structure.
a. Suppose that you have the peptide Ala-Gly-Tyr-His-Leu and you treat it with FDNB and then 6M HCl. Draw the structures of all the products that you will have in solution (assume all reactions to go to completion).
Determine the pI of the peptide H2N-Ala-Lys-Ser-Arg-COOH at pH 11, please explain why some pKas are used in the solution of the problem while others are not.
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

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