L 3 0Question 1The amino acid Asp is triprotic with pK₁ -1.88, pK₂-9.60, and pK; -3.65.What is the charge of the a-NH₂ functional group at pH 11? [Select]What is the net charge of Asp at pH 11? | Select]Question 2What is the isoelectric point (pl) for the dipeptide HKIF?For calculation of this question, use the pK, values found here: https://www.chem.ucalgary.ca/courses/351/Carmv5th/Ch27/27-1-42.htmleThe pka values for the N and C-termini are 8.00 and 4.00, respectively.Answers should have correct significant digits.

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Answered: 0 Question 1 The amino acid Asp is…

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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80mL of a 0.3M solution of hexapeptide Leu-His-Cys-Glu-Asn-Arg is adjusted to pH=pl. The solution is then titrated with 0.2M HCI to a final pH of 2.1. Sketch the titration curve, labelling the pH and volume axes. Indicate the volume of HCl needed to reach each relevant pKa value and equivalence point(s). Relevant pka values are: 2.1, 4.3, 6.0, 8.3, 9.8, and 12.5.
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?
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
Predict the direction of migration for the following amino acids in solutions of the specified pH. Write Isoelectric, if no migration occurs: Lys at pH=12 (pk values: 2.2; 9.2; 10.8) Glu at pH= 2.0 (pk values: 2.1; 9.5; 4.1) Leu at pH= 6.0 (pk vaues: 2.3; 9.7)
What is the dissociation equilibrium constant of a protein if the concentration of free ligand is 3.0um when the fraction of bound sites is 0.6
The equilibrium constant for the hydrolysis of the peptide alanylglycine (Gly-Ala in the reaction from Part B) by a peptidase is K = 9.0 × 10² at 310 K. Calculate AG for this reaction. Express the Gibbs free energy to three significant figures. AG = Submit ΠΑΠΙ ΑΣΦ Request Answer ? kJ/mol Keq [Gly] [Ala] [Gly-Ala]
What is the net average charge on the predominant form of lysine at pH values of (a) 2.0, (b) 5.0 and (c) 7.0? CLUE: draw the structure of lysine and show its different charged forms; then consider in which pH domains the pKa values for deprotonation/protonation occur.
Calculate the isoelectric point of the tetrapeptide Ser-Leu-Phe-Pro at pH 7.0
Which intermolecular forces are important in acetic acid, CH3 –(C=0)-oh? A particular amino acid contains a- CHNH3+ group. Is this amino acid more likely to be found on the inside or the outside of the folded protein? Briefly explain. The addition of ethanol, CH3CHOH, t 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.
Draw the structure of the pentapeptide Gln-Trp-His-Glu-Tyr that would predominate in acqueous solution at pH=10.3. (Relevant pKa values are: 2.2,4.3,6.0,9.8 and 10.1)
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
Calculate the overall net charge of the following polypeptide at pH = 2.0 Gly-Pro-Glu-Asp-Leu-His-lle-Gln-Asn-Phe A) +1.76

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