For the electrophoresis at 25°C of two proteins, in amedium with a viscosity of 0.001kg/m-s, thefollowing variation of dispersion by diffusion with timewas obtained.t (h)00.5124Dispersion (cm)Proteín A Proteín B00.0530.0750.1060.15100.0440.0620.0870.123Indicate through calculations, which of the proteinspresented were those treated by electrophoresis:Ovalbumin (45,000), Collagen (345,000), LmG(150,000) and Keratin (65,000).

Electrophoresis is a technique used in biotechnology to separate and analyze biological molecules…

Answered: For the electrophoresis at 25°C of two…

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

A large chaperone protein complex GroEL is approximately 16 nm in diameter. When it is dissolved in water at 300 K, estimate the average time it will take for GroEL to diffuse a distance of 500 nm (0.5 micron). The viscosity of water is 10-3 Pa*s.
A new protein namely protein X has been isolated by molecular biologists. The protein is shown to have a spherical shape and a radius of 12 nm. Before they could measure its diffusion coefficient at 25°C, their device breaks. However, they have data from a previous measurement taken using the same device, at 25°C which showed diffusion coefficient of albumin (spherical with R=3 nm, M= 68,000 g/mol) to be 6.8x10-7 cm2/s. Determine the diffusion coefficient of protein X.
Molecular diameters of proteins IgG and TNFα are 11.2 nm and 4.4 nm, respectively. The diffusion coefficient of IgG in a dilute aqueous solution at 37oC is 2.8 ⤬ 10-7 cm2/s. Estimate the diffusion coefficient of TNFα in a dilute aqueous solution at the same temperature.
A sample of a protein is analyzed by CE using a neutral-coated capillary with a total length of 25.0 cm and a distance to the detector of 22.0 cm. Using an applied voltage of 20.0 kV, the protein was detected at a migration time of 16.2 min. The diffusion coefficient for the protein is 2.4 x 10-7 cm?/s. (a) Calculate the apparent electrophoretic mobility of the protein. (b) Calculate the expected number of theoretical plates for the analysis.
The diffusivity of amino acids in polyacrylamide gel is approximately 1x10^-9 cm2./s calculate the initial flux of amino acids, give an instantaneous gradient of (20g/cm 3 )/8cm Why is polyacrylamide gel is used in electrophoresis?
The A280 of a protein sample loaded onto a gel was determined to be 0.767 (1.00 cm path length, after subtracting the blank). The total volume of this sample was 428 µL. 19.0 µL of this protein sample was mixed with 19.0 µL of 2X laemalli sample buffer and then 12.0 µL of the entire sample was loaded into the gel and electrophoresed. Calculate the amount of protein that was loaded into the gel (in µg).
Consider the following protein mixture: Protein A B C D Molecular Weight (kDa) 50 150 200 350 Affinity to Metal ion === Zn²+ === 1. Using hydrophobic interaction chromatography, the protein that will be eluted last is [Select] 2. Using affinity chromatography, the protein that will be eluted last in a Zn²+-containing column is 3. The protein with the fastest migration towards the anode in SDS-PAGE is [Select] IpH value 7 3 9 5 [Select] [Select] 4. Using a buffer solution with a pH of 4, the protein that will bind to an anion exchanger is 5. The protein that will be eluted last in a gel filtration column is [Select] 6. Using isoelectric focusing, the protein that will have a protein band nearest to the cathode (negative electrode) is [Select] % Hydrophobicity 20 45 75 55
A series of standard proteins and an unknown enzyme were studied by gel filtration on a Sephadex G200 (the 200 refers to the maximum pore size in kDa) column. The elution volume Vel for each protein is given in Table 1 below. (a) Plot the data in the form of log Mr versus elution volume. From the line of best fit through the points for the standards, determine the Mr of the unknown enzyme. Explain why ferritin and ovomucoid behave anomalously. Table 1 - The Vel versus Mr data Protein Mr Vel (mL) Blue dextran* Lysozyme Chymotrypsin Ovalbumin Serum albumin Aldolase Urease Ferritin# Ovomucoid# Unknown 1,000,000 14,000 25,000 45,000 68,500 150,000 500,000 700,000 28,000 ⎯ 85 200 190 170 150 125 90 92 160 139 *Blue dextran is not a protein but a high-Mr carbohydrate that has a covalently bound blue dye, and it elutes with the void volume of the column. # Do not…
Two co-op students at your start-up company have been asked to evaluate the rate of reaction occurring in a transparent gel particle containing immobilized mouse melanoma cells. The equation for the reaction rate ris is: Vmax T'As Km+CAs where R=3.2 mm, Vmax= 0.12 gmol s' m3, CAS = 41 gmol m3, and Km=0.8 gmol m3. One student reports a reaction rate of 1.6x10 gmol st; the other reports 1.6x10 1º gmol s1. You left your calculator on the bus this morning, but must know quickly which student is correct. Use an order-of- magnitude calculation to identify the right answer. Which student is correct?
What is the diffusion coefficient of a membrane-bound protein of molar mass 79,300 daltons at 37°C if the viscosity of the membrane is 1 poise (0.10 N-s-m-2)? Assume that this protein is an unhydrated, rigid sphere that has a density of 1.4 g.cm-3. 4.0 12.83e-9 X m².s-1 What is the average distance traveled by this protein in 2.3 s? 4.0 1.7e9 X Å
From this standard curve and chart below, does the separation of molecules in the mixture appear successful from the gel filtration? Is there a clearlydefined separation between molecules? Explain your conclusions. Parameters required for calculation of coefficient (Kd) for unknown protein Volume eluted (mL) Which variable does this volume represent in the equation for Kd? Fraction with maximal DNP-Aspartate detected 36 Vt Fraction with maximal Protein detected 24 Ve Fraction with maximal Blue dextran detected 6 Vo
Suppose you calculate that you can load 2000ng of Sample A and suppose your concentration of Sample B is 450ng/uL. How many uL of Sample B would you need to load the same amount of protein into the gel?

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