on 2 of 3HintResumeQuestionEach ionizable group of an amino acid can exist in one of two states, charged or neutral. The electric charge on the functionalgroup is determined by the relationship between its pK, and the pH of the solution. This relationship is described by theHenderson-Hasselbalch equation.Histidine has three ionizable functional groups. Complete the equilibrium equations by assigning the proper pK, for eachionization and the net charge on the histidine molecule in each ionization state.HHH,N*-C-C-OHH,N*-C-C-o-H,N*-C-C-o-H,N-C-C-o-CH,CH,CH,CH,HNHNN'-NH-NH-NH-NH.........Answer Bank-2pK, = 9,17-1+1pKa = 6.0pK, = 7.59pK, = 1.8of Fi..docxDDDIIF11F10FBF7888F680F5F4F3&%24674.5UR11o=U

pH is the measure of the strength of H+ ion or Hydronium ions in solution. pOH is the…

Answered: molecule in each ionization state. H||…

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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Each ionizable group of an amino acid can exist in one of two states, charged or neutral. The electric charge on the functional group is determined by the relationship between its pKa and the pH of the solution. This relationship is described by the Henderson-Hasselbalch equation.(a) Histidine has three ionizable functional groups. Write the equilibrium equations for its three ionizations and assign the proper pKafor each ionization. Draw the structure of histidine in each ionization state. What is the net charge on the histidine molecule in each ionization state?(b) Draw the structures of the predominant ionization state of histidine at pH 1, 4, 8, and 12. Note that the ionization state can be approximated by treating each ionizable group independently.(c) What is the net charge of histidine at pH 1, 4, 8, and 12? For each pH, will histidine migrate toward the anode (+) or cathode (−) when placed in an electric field?
Polymer beads (resin) made of DEAE (diethylaminoethyl) cellulose are packed in an ion exchange column. The total mass of beads in the column is 8.47 kg. On average, each bead weighs 0.0023 g and has an average of 18.4 * 10° positively charged amine groups that can adsorba negatively charged protein that passes through the column. A solution containing 2.07 mg/L of a protein is maintained at pH 6.3 and is passed through the ion exchange column at 0.215 L/min. The protein has a molecular weight of 154,000. The pk, of the amino groups on DEAE cellulose is 7.1, and the pl of the protein is 5.6. 2. A. How long can the column be operated before reaching 80% capacity (i.e., 80% of the amino groups on DEAE are bound to the protein through an ionic bond)? You may assume that one protein attaches to one + charge on the beads (although it's possible that proteins attach to more than one + charge). B. After reaching 80% capacity, explain what you would do to release the protein attached to the…
A 100 ml solution of 0.1 M amino acid (AA) at ph 1.0 was titrated with NaOH solution. The pH was monitored, and the results were plotted on the graph. The keypoints in the titration are designated I to VII. What is the possible identity of the amino acid? What is the isoelectric point of AA? what is the pKa corresponding to the dissociation of the alpha carboxylic group? Region/point where AA is predominantly present as a (-1) charged species? The effective buffering range for the amino acid in the acidic region? Region/point where the solution has 50:50 percent mixture of the (0) and (-1) species
The following amino acid is dissolved in solution at pH 7.4. HC H' + CH CH₂ H/ H+ HC a. Which amino acid is this? (all lower case) N- H CH CH₂ b. What is the pKa of its ionizable side chain? (Use the value from the textbook.) c. What is the ratio of the uncharged to the charged form at pH 7.4? (write answer as number with one decimal place, ex 2.5 or 0.2 or 50.0 with an implicit "to 1")
Sketch a titration curve for aspartic acid, andindicate the pKa values of all titratable groups. Also indicate thepH range in which the conjugate acid–base pair +1 Asp and 0 Aspwill act as a buffer
Determine the net charge (to the nearest integer) on the following peptide at pH 5 AND pH 12. Estimate the isoelectric point (pl) for this peptide: H2N-Leu-Gly-Lys-Glu-COOH Assume the pK,s for functional groups are: alpha-amino 6. alpha-carboxy sidechain-amino (Lys) 10.5 sidechain-carboxy (Glu) 4.2 O Net charge at pH 5 and 12 is 0 and -2, respectively, pl =6.6 O Net charge at pH 5 and 12 is 0 and -2, respectively, pl =3.1 O Net charge at plH 5 and 12 is +2 and -1, respectively, pl =7.5 O Nct charge at pH 5 and 12 is +1 and -1. respectively,. pl -4.5 2.
A protein gives, under conditions of buffer composition, pH, and temperaturethat are close to physiological conditions, a molecular weight by size exclusion measurements of 140,000 g/mol. When the same protein is studiedby SDS gel electrophoresis in the absence or presence of the reducing agent β-mercaptoethanol (BME), the patterns seen, respectively, in lanes A and B are observed. Lane C contains standards of molecular weight indicated. From these data, describe the native protein, in terms of the kinds of subunits present, the stoichiometry of subunits, and the kinds of bonding(covalent, noncovalent) existing between subunits.
Diethylaminoethyl cellulose is a positively charged resin used in ion-exchange chromatography with a pKa is about 11. A negatively charged protein with an isoelectric point of 5.0 is applied to the column in a buffer at pH 7 and containing 0.1 M NaCl. Which of the following conditions is most likely to weaken the interaction between the protein and the resin? A Raising the pH to 8 and decreasing the NaCl to 0.05 M B Raising the pH to 8 and increasing the NaCl to 0.2 M C Lowering the pH to 6 and decreasing the NaCl to 0.05 M D Lowering the pH to 6 and increasing the NaCl to 0.2 M
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.
To calculate the isoelectric point of amino acids having other ionizable functional groups, we must also take into account the pk, of the additional functional group in the side chain. For an acidic amino acid (one with an additional acidic OH group): For a basic amino acid (one with an aditional basic NH group): pK, (a-COOH) + pK, (second COOH) - pKa (a-NH3") + pK, (side chain NH) pl = a. Indicate which pK, values must be used to calculate the pl of each of the following amino acids: [1] glutamic acid; [2] lysine; [3] arginine. b. In general, how does the pl of an acidic amino acid compare to that of a neutral amino acid? c. In general, how does the pl of a basic amino acid compare to the pl of a neutral amino acid?
Amino acid Cys has ionizable groups with pKa values 2.0, 8.0, and 10.0. Determine the charge on the Cys at the following pH. Be sure to write the charge in fraction with sign in front (for example, +1/2, -1/5, and +7/8). Charge when pH is at 1.0? _________ Charge when pH is at 9.0? _________ Charge when pH is at 8.0? _________ Charge when pH is at 10.0? _________
Indicate which of the amino acid residues in the following peptide sequence contains a group that has a positive charge for its most likely charge state at pH 10. Asp-Tyr-Lys-GIn-Thr-Ile-Phe-Met-Ser (If none of the amino acids fit the criterion, select "none".) Asp Tyr ооооооооо Lys Gln Thr lle Phe Met Ser none

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molecule in each ionization state. H|| H,N*-C-C- OH H|| H,N-C-C-0- H I H,N-C-C-0- H,N-C-C-C CH, CH, CH2 CH, HN HN -NH -NH -NH -NH Answer Bank -1 +1 +2 PK, = 1.8 -2 PK, = 9,17 PK, = 7.59 %3D pK, = 6.0 %3D .....