A spheroidal bacterium with a diameter of 1.0 mm (micrometer, 1 mm = 10-6) contains 25,000 molecules of the protein hexokinase. What is the molar concentration of the protein inside the cell?
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A spheroidal bacterium with a diameter of 1.0 mm (micrometer, 1 mm = 10-6) contains 25,000 molecules of the protein hexokinase. What is the molar concentration of the protein inside the cell?
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- A 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?Which of the following is NOT a unit of concentration? All of these options are units of concentration. mM Moles/Liter Molar You gathered your data from Lab , 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. A 7 fold B 150% C 15 fold D 70%A solution contains a mixture of four proteins: urease, ovalbumin, lysozyme, and alkaline phosphatase. The proteins have the following properties. Molecular weight (Daltons) Protein pl Urease 483,000 5.0 Ovalbumin 45,000 4.6 Lysozyme 86,000 11.0 Alkaline 86,000 4.6 Phosphatase Based on the information provided, what type of chromatography (gel permeation or ion exchange) could be used to separate: a) Lysozyme from Alkaline Phosphatase. Briefly explain your answer. b) Ovalbumin from Alkaline Phosphatase. Briefly explain your answer. c) Which of the four proteins would be bound to a cation exchanger equilibrated at pH 5? d) Briefly explain your answer to part c).
- Using ultrafiltration, you concentrate a solution of Protein X as follows: Initial volume protein X = 300 mL Initial concentration protein X = 12 mg/mL Final volume protein X = 15 mL What's the final concentration of protein X in mg/mL?Four proteins Cytochrome C (pI=10.2) Myoglobin (pI=7.2), Hemoglobin (pI = 6.8) and Serum Albumin (pI= 4.8) were used in our gel electrophoresis lab exercise. If the electrophoretic separation is carried out at pH 7.0, which protein would move toward the negative electrode? Cytochrome C Myoglobin HemoglobinA mixture of proteins contains Pepsinogen (35 kDa), Fumarase (49 kDa), Transferrin (80 kDa) and Thyroglobulin (340 kDa). Rank these proteins based on the order of their elution from a gel filtration column (1 being the first one to elute and 4 as the last one). Throglobulin Pepsinogen Fumarase Transferrin
- The α-amylase (α-AM) enzyme secreted by Aspergillus has an isoelectric point of approximately 4.2. If the purification method in problem 1 operates at pH 6.5, would the protein carry a positive charge, negative charge, or net zero charge?a) 1,3-Diisopropylurea is a relatively small, very hydrophobic molecule. Suppose that the [1.3- diisopropylurea] outside of a cell is 5*10-° M, and the [1,3-diisopropylurea] inside the cell is 2*10-5 M. If the diisopropylurea were to move out of the cell, what transport process would be used? Circle the correct answer from the list below. 9) - Active transport: receptor mediated endocytosis - Passive transport: simple diffusion %3D - Passive transport: osmosis - Active transport: protein pumps proog - Active transport: phagocytosis - Passive transport: facilitated diffusion - Active transport: pinocytosis b) In terms of rate of transport of a molecule across a membrane, what is the difference betwee passive and active transport? tassive tranport is the movement a concentration gradient ronm higher to lower concentr without the use QP huolecules down ene Active transport is the movement of molecules over a concentraleon gradient concentration with the we బూబ ర active transport is of…Figure 3: ● ● ● ● ● ● KDa ● 97.4 66.2 45.0 ● 31.0- 21.5 14.4 S-1 p-1 S-2 2-0 This figure was generated by centrifuging a pura sample of protein, removing the supernatant, and resuspending the pellet in the same volume as the supernatant to allow direct comparison. The supernatant and pellet samples were then prepared for SDS-PAGE identically and run via normal SDS-PAGE procedures. In the figure, "s" means supernatant and "p" means pellet. The text or number after the dash represents a different condition. For example, s-1 and p-1 are the supernatant and pellet samples under condition 1. It is not shown, but under wild-type conditions, essentially all of the protein is found in the supernatant. S-3 ● What does the intensity of each band represent? ● Would you find soluble protein in the supernatant or pellet? Why? Would you find aggregated protein in the supernatant or pellet? Why? For each condition (there are 5 different conditions), is there a higher percentage of the total protein…
- What are the example of nanostructures? Give at least ten and define each Note: [Do not copy on Google!]You 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 foldA 20µL unknown protein was mixed with 80µL of water. Then, 10µL of this mixture was added with 10µL Bradford reagent and diluted with water to a total volume of 100µL. The absorbance at 595 nm shows 0.08 units. Solve for the protein concentration (in mg/mL) of the original unknown protein. How much protein (in mg) is in the 20uL sample? Express your answer in 3 significant figures.