An Fab fragment binds to lysozyme with a dissociation constant of K4 = 10 M. A 1 nM (10 M) solution of lysozyme is treated with increasing concentrations of the Fab fragment. At what concentration of added Fab will half of the lysozyme be bound to the Fab? nM
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![An Fab fragment binds to lysozyme with a dissociation constant of K4 = 10-¹1 M. A 1 nM (109 M) solution of lysozyme is
treated with increasing concentrations of the Fab fragment. At what concentration of added Fab will half of the lysozyme be
bound to the Fab?
[F] =
nM](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fc4dc380c-a82f-4308-8d95-1a09bead5fa9%2F072f2a38-7f2a-4aa6-a43b-e331ff6d52f7%2F0q1ejm_processed.jpeg&w=3840&q=75)
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- Electrophoresis is performed at PH 6.8 on a mixture of mutated hemoglobin that differ from normal haemoglobin (Hb) only by the substitution of one amino acid- Hb X: Val replaced par Glu - Hb Y: Asp replaced by Leu - Hb Z: Glu replaced by Lys What will be the order of migration between cathode and anode of these mutated Hb compared to normal Hb? Justify your answer.What is the expected outcome of the ion exchange chromatography using lysozyme as outlined above? Will the protein be separated successfully or not using the materials stated in the above? Provide a brief explanation to your reasoning please answer correctly, not written assigmentA spheroidal bacterium with a diameter of 1.0 μm (micrometer, 1 μm = 10-6) contains 25,000 molecules of the protein hexokinase. What is the molar concentration of the protein inside the cell?
- A mixture of proteins having molecular weights of 50 to 200 kDa can be fractionated linearly using a GFC column with an exclusion limit of at least _____.a. 25 kDab. 50 kDac. 125 kDad. 200 kDapls explain whyYou gathered your data from Lab 4, and found the following values: Total Activity of lysozyme in HEW: 14 units Total Activity of lysozyme in carb 1: 21 units Total amount of protein in HEW: 70 mg Total amount of protein in Carb 1: 15 mg Calculate the extent of purification of lysozyme in Carb 1. 150% 7 fold 70% 15 foldConsider the following properties of the protein components of a sample mixture as provided in the table below: 1. if the mixture is subjected to gel filtration chromotography which protein component elute first? 2. if the mixture is subjected to isoelectric focusing which protein will stop m oving nearest to the positive electrode? 3. if the mixture is subjected to cation-exchange chromotography using a buffer at ph 7 which protein will bind to the resin? 4.if the mixture is subjected to SDS-PAGE which protein will be at bottomost portion of gel? 5.if the mixture is subjected to hydrophobic interaction chromotography which protein will bind most strongly to the resin?
- You want to treat 10 mL of HL-60 cells with cycloheximide in order to determine the half-life of a newly discovered protein. In order to do this, the final concentration of cycloheximide needs to be 90 µM. How much of a 150 mM stock solution of cycloheximide should you add to your cells?Identify the following by describing their functions: EF-G, EF-Tu, EF-Ts, EF-P, and peptidyl transferaseUpon doing the experiment of Protein Denaturation, what could be observed in the precipitation of heavy metal ions if an albumin solution in a solution is dropped with drops of silver nitrate and then it will be shaken? Explain.
- How many copies of a protein need to be presentin a cell in order for it to be visible as a band on an SDSgel? Assume that you can load 100 μg of cell extract ontoa gel and that you can detect 10 ng in a single band by sil-ver staining the gel. The concentration of protein in cellsis about 200 mg/mL, and a typical mammalian cell has avolume of about 1000 μm3 and a typical bacterium a vol-ume of about 1 μm3. Given these parameters, calculatethe number of copies of a 120-kd protein that would needto be present in a mammalian cell and in a bacterium inorder to give a detectable band on a gel. You might try anorder-of-magnitude guess before you make the calcula-tions.A number of techniques can separate proteins on the basis of their differences in mass. Describe the use of two of these techniques, centrifugation and gel electrophoresis. The blood proteins transferrin (MW 76 kDa) and lysozyme (MW 15 kDa) can be separated by rate zonal centrifugation or SDS-polyacrylamide gel electrophoresis. Which of the two proteins will sediment faster during centrifugation? Which will migrate faster during electrophoresis?a. An oligopeptide ALVGALGATPTPQMWSHSWRGVSIKS was digested with trypsin.Which method would be most appropriate for separating the products: ion exchange or gel filtration chromatography? Explain.b. Suppose that the peptide was digested with cyanogen bromide. What would be the optimal separation technique? Explain