Homework Answers
Membrane rafts are small (10-200 nm), heterogeneous, highly dynamic, sterol and sphingolipid enriched domains that compartmentalize cellular processes.
Biochemically, membrane rafts are isolated by solubilization in ice-cold Triton X-100 and separation of the low-buoyant density fractions from soluble material on sucrose density gradients. Raft membrane is separated using the Density - gradient centrifugation.
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Raft membranes can be isolated by: Polyacrylamide gel electrophoresis а. Gel Filtration chromatography b. HPLC C....
Exercise IV. Fill in the Blank 1. The method of Centrifugation, polyacrylamide gel electrophoresis, western blotting,...
Exercise IV. Fill in the Blank 1. The method of Centrifugation, polyacrylamide gel electrophoresis, western blotting, affinity purification) is the most widely used technique for determining the approximate molecular weight of a protein. 2. (Centrifugation, affinity chromatography, sonication, gel electrophoresis) is a method in which macromolecules are separated due to their size, charge, and other physical properties 3. SDS-PAGE is a form of electrophoresis in the presences of a/an (acidic solution, basic solution, anionic detergent, cationic detergent). 4. SDS not...
Can someone answer the question and provide a short explanation? Thanks! Which of the following statements...
Can someone answer the question and provide a short explanation? Thanks! Which of the following statements is NOT correct regarding protein seperation techniques? A) Size-exclusion chromatography works on the same principle as polyacrylamide gel electrophoresis B) Specific antibodies are required for immunoblotting, antibody affinity chromatography as well as immunoprecipitation C) Two-dimensional gel electrophoresis is conceptually the same as combining gel filtration chromatography and ion exchange chromatography D) Western blotting is a useful technique to isolate proteins for use in downstream...
In Gel Filtration Chromatography, polyacrylamide beads and phosphate buffer were used. We wanted to separate Blue...
In Gel Filtration Chromatography, polyacrylamide beads and phosphate buffer were used. We wanted to separate Blue Dextran (2 mDa/blue), BSA (70 kDa, no color), myoglobin (17 kDa, reddish/brownish), and yellow food coloring (500 Da, yellow). For some reason, some fractions we collected earlier contained 3 substances (Blue Dextran, BSA, and myoglobin) together. A little later, fractions collected contained BSA and myoglobin, but the color of them was clear. Why did fractions collected earlier contain Blue Dextran, BSA, and myoglobin though...
parts a,b, c please 3. Sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis a. After pouring the...
parts a,b, c please
3. Sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis a. After pouring the SDS polyacrylamide gel, you realize that instead of 2 ml, you used 4 ml of 30% acrylamide/bisacrylamide solution for the preparation of the separating gel (in both cases for 5 ml, total gel volume). How would this affect the separation of your proteins during SDS PAGE? Explain your answer! b. You have to remake the gel and are now making sure just to add...
The PCR procedure can be performed with fluorescently labeled primers and polyacrylamide gel electrophoresis (PAGE). What...
The PCR procedure can be performed with fluorescently labeled
primers and polyacrylamide gel electrophoresis (PAGE). What would
be the advantage of this procedure over agarose gel analysis?
PAGE allows for higher resolution than the agarose gel
procedure.
The PAGE procedure is faster than that using agarose gel
electrophoresis.
The labeled primers are less expensive because they are used at
a lower concentration in the reaction mix.
The PAGE procedure is less prone to contamination
Case Study 12-2 A 7-month-old child...
Gel electrophoresis. Polypeptides can be separated by electrophoresis according to their relative content of acidic and...
Gel electrophoresis. Polypeptides can be separated by electrophoresis according to their relative content of acidic and basic residues. The isoelectric point (pI) of a polypeptide is the pH at which its net charge is zero. (See Fig 3.11 of your textbook). A) At physiological pH (= 7.4), what is the net charge on the tripeptide Asp-Arg-Glu-His? B) Calculate the pI of this tetrapeptide. [Hint: Using the pK, values in Table 2.1 and the Henderson-Hasselbalch equation, determine the pH when the...
4. (Challenge) You are purifying a protein from the brain of patients with an unusual type of...
4. (Challenge) You are purifying a protein from the brain of patients with an unusual type of dementia triggered by a coronavirus and you hypothesize that this protein may be a signature molecule of this type of dementia. To pursue this hypothesis, you collect brain tissue from patients post mortem, do differential centrifugation, density gradient centrifugation, CM (carboxymethyl cellulose) ion exchange chromatography and gel filtration. You then assess the purity of your protein using both native and SDS gel electrophoresis. The...
15. In which of the following procedures does the sample stop moving until conditions change? i....
15. In which of the following procedures does the sample stop moving until conditions change? i. Size exclusion chromatography ii. SDS-electrophoresis iii. Isoelectric Focusing iv. Density gradient centrifugation V. Rate-zonal centrifugation a. ii, iii, and v. b. iii, and iv. c. ii, iv, and v. d. only iii e. all excepti. 16. or the following types of separation, which gives one the best chance of obtaining a protein in its properly folded state? a. Affinity Chromatography b. SDS Electrophoresis c....
Problem 1. (15 pts) Multiple Choice Which of the following methods can be used to purify...
Problem 1. (15 pts) Multiple Choice Which of the following methods can be used to purify large amounts of proteins a. Hydrophobic chromatography b. Precipitation c. Equilibrium dialysis d. Polyacrylamide gel electrophoresis e. Ion exchange chromatography f. a, c, e g. a, b, c, d h. a, b, c, e i. All of the above Circle the one correct answer. a. Beta sheets are stabilized by H-bonds b. Ramachandran plots are determined by steric clashes between side chains and the...
3 of 5 Part II (25 points) Problem 3 (25 pts) Components from the cytosol can...
3 of 5 Part II (25 points) Problem 3 (25 pts) Components from the cytosol can be separated on a sucrose gradient by equilibrium equilibrium (Remember: a similar method was used to demonstrate that DNA replication is semi- conservative). After centrifugation, heavy (high density) protein complexes will sediment further away from the top of the gradient than light (low density) complexes. When the gradient is collected into fractions of increasing density, protein complexes that migrated at different level of the...
Exercise IV. Fill in the Blank 1. The method of Centrifugation, polyacrylamide gel electrophoresis, western blotting, affinity purification) is the most widely used technique for determining the approximate molecular weight of a protein. 2. (Centrifugation, affinity chromatography, sonication, gel electrophoresis) is a method in which macromolecules are separated due to their size, charge, and other physical properties 3. SDS-PAGE is a form of electrophoresis in the presences of a/an (acidic solution, basic solution, anionic detergent, cationic detergent). 4. SDS not...
parts a,b, c please
3. Sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis a. After pouring the SDS polyacrylamide gel, you realize that instead of 2 ml, you used 4 ml of 30% acrylamide/bisacrylamide solution for the preparation of the separating gel (in both cases for 5 ml, total gel volume). How would this affect the separation of your proteins during SDS PAGE? Explain your answer! b. You have to remake the gel and are now making sure just to add...
The PCR procedure can be performed with fluorescently labeled
primers and polyacrylamide gel electrophoresis (PAGE). What would
be the advantage of this procedure over agarose gel analysis?
PAGE allows for higher resolution than the agarose gel
procedure.
The PAGE procedure is faster than that using agarose gel
electrophoresis.
The labeled primers are less expensive because they are used at
a lower concentration in the reaction mix.
The PAGE procedure is less prone to contamination
Case Study 12-2 A 7-month-old child...
Gel electrophoresis. Polypeptides can be separated by electrophoresis according to their relative content of acidic and basic residues. The isoelectric point (pI) of a polypeptide is the pH at which its net charge is zero. (See Fig 3.11 of your textbook). A) At physiological pH (= 7.4), what is the net charge on the tripeptide Asp-Arg-Glu-His? B) Calculate the pI of this tetrapeptide. [Hint: Using the pK, values in Table 2.1 and the Henderson-Hasselbalch equation, determine the pH when the...
15. In which of the following procedures does the sample stop moving until conditions change? i. Size exclusion chromatography ii. SDS-electrophoresis iii. Isoelectric Focusing iv. Density gradient centrifugation V. Rate-zonal centrifugation a. ii, iii, and v. b. iii, and iv. c. ii, iv, and v. d. only iii e. all excepti. 16. or the following types of separation, which gives one the best chance of obtaining a protein in its properly folded state? a. Affinity Chromatography b. SDS Electrophoresis c....
Problem 1. (15 pts) Multiple Choice Which of the following methods can be used to purify large amounts of proteins a. Hydrophobic chromatography b. Precipitation c. Equilibrium dialysis d. Polyacrylamide gel electrophoresis e. Ion exchange chromatography f. a, c, e g. a, b, c, d h. a, b, c, e i. All of the above Circle the one correct answer. a. Beta sheets are stabilized by H-bonds b. Ramachandran plots are determined by steric clashes between side chains and the...
3 of 5 Part II (25 points) Problem 3 (25 pts) Components from the cytosol can be separated on a sucrose gradient by equilibrium equilibrium (Remember: a similar method was used to demonstrate that DNA replication is semi- conservative). After centrifugation, heavy (high density) protein complexes will sediment further away from the top of the gradient than light (low density) complexes. When the gradient is collected into fractions of increasing density, protein complexes that migrated at different level of the...
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