A researcher is preparing a reaction mixture to test the activity of a protein.They combine the required reaction components, which contained in a final 100 ml reactionvolume 200 mM NaCl, unknown concentrations of acetic acid and acetate anions and a total [H+]concentration of 790 ricromolar.Can you determine the pH of the solution?Provide the answer to one decimal place.Note: You may need to round the numbers to get the required answer.100 StripspH indicator strips non-bleedingpHpH 0-14EM-ReagentsDip in-read while still moist.immerse in weakly-buffered solutions unethere is no further color change (1-10 min)3756

pH is the negative log of H+ concentration. The H+ concentration should be in molar (M). 1 μM = 10-6…

Answered: A researcher is preparing a reaction…

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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Similar questions

If a data from an enzyme experiment is plotted as a Lineweaver - Burk plot, and the Vmax is 0.02 sec/mol, and x-intercept is -2.5 mM-1, then what is the KM value?
A 100 mL of 0.1 M amino acid at pH 1.0, whose pka for the carboxyl group is less than the pKa of the R-group, was titrated with NaOH solution. The pH was monitored, and the results were plotted on a graph, as shown below. The key points in the titration are designated A to G. 12 10 8 pH 6 4 2 0 A B 0.5 с D E F 1.5 2 2.5 Equivalents of OH 1. What is the possible identity of the amino acid? [Select] 2. What is the isoelectric point of the amino acid? [Select] 3. What is the pka corresponding to the deprotonation of the alpha-amino group? [Select] 4. Region/ point where the amino acid is predominantly present as a (-2)-charged species. [Select] 5. The effective buffering range for the amino acid in the basic region. [Select] G 3
A purified protein sample was used in a reaction, resulting in an activity of 696.7 nmol min-1. The reaction volume was 145.0 µL and the final volume before loading the plate was 1,050 µL. The total reaction time was 4.25 min. The amount of protein used in the reaction was 4.270 µg. Calculate the specific activity of the sample (in nmol min-1 µg-1).
Using your stock solution of 2 M glucose, you need to prepare the following series of glucose solutions for use in an experiment 0.8; 1.5, 1.75 and 2 M. Complete the table to show how you would dilute the sucrose to make 100ml of each of the solutions above.
Highlight your values of A,B,C and D. For your question: A mL of B mol/L sodium phosphate solution is combined with C mL of D mol/L calcium bicarbonate. (Calcium bicarbonate is soluble.) A mL B mol/L C mL D mol/L 75.0 ml 0.300 67.5 0.350 Before you begin your reaction, you must accurately produce 1.500 L of your sodium phosphate solution from sodium phosphate trihydrate solid. Write out a procedure to explain all the steps you will take in the lab when making the solution to ensure that your solution concentration is accurate. Please include calculations that show the required mass of solid. Also include the correct names of all equipment used.
Given a stock protein solution with a concentration of 6 mg/ml, determine the protein concentration of a solution made by mixing 5 μl of the stock with 5 μl of a buffer.
An amino acid mixture consisting of lysine,leucine, and glutamic acid is to be separated by ion-exchangechromatography, using a cation-exchange resin at pH 3.5, with theeluting buffer at the same pH. Which of these amino acids will beeluted from the column first? Will any other treatment be neededto elute one of these amino acids from the column?
Can you please explain how to approach this problem?
Solve the following and explain the complete process.
From a kinetics experiment, the Vmax was determined to be 450µM∙min-1. For the kinetic assay, 0.1mL of a 0.05mg/mL solution of enzyme was used, and the enzyme has a molecular weight of 125,000 g/mole. Assume a reaction volume of 700µL. Calculate the kcat (in sec-1) for the enzyme.
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…
Describe the preparation of 2.00 L of 0.100 M glycine buffer, pH 9.0, from glycine and 1.00 M NaOH. What mass of glycine is required, and what volume of 1.00 NaOH is required? The appropriate pKa of glycine is 9.6

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