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- Please describe the protein purification process with the aim of purifying a protein which locates on nucleus membrane.The amino acid of a transmembrane protein was analyzed with a hydrophobicity (Kite-Doolittle) plot as shown below. Based on the graph on the left below how many times does the protein predicted pass through the membrane? TIBS 15-MARCH 1990 RVMV. Raw format file: RVMV. Protein Length: 318 Check: 7395 4. RVMV. Raw format file: RVMV. Protein Length: 318 Check: 7395 3 3 2- 2 -2- --3 -2 50 100 150 200 250 300 50 100 150 200 250 300 Residue Number Residue Number Figure 2 Figure 4 The Kyte-Doolittle (KD)12 hydrophobicity plot (w 9) of the M-chain of Rsp. viridis. The Sieved-Kyte-Doolittle (SKD)* hydrophobicity plot (w = 9) of the M-chain of Rsp. viridis. 1 time 3 time 5 times 7 times Other Mesh SievedExample Problem: FRAP Data Interpretation The diffusion rate of four different membrane proteins (A, B, C, and D) was measured using a FRAP experiment with purified liposomes. The FRAP recovery curves are shown below. Fluorescence intensity ROI A 3 Time B Time Post-bleaching imaging с Time D Time Pre-bleaching Bleaching imaging imaging (a) Which membrane protein exhibits the higher rate of diffusion in the lipid bilayer? A or B? C or D? (b) Explain the most likely cause of the difference in the recovery curves for proteins A and C.
- Consider a polymeric membrane within a 6 cm diameter stirred ultrafiltration cell. The mem- brane is 30 μm thick. The membrane has pores equivalent in size to a spherical molecule with a molecular weight of 100,000, a porosity of 80%, and a tortuosity of 2.5. On the feed side of the membrane, we have a solution containing a protein at a concentration of 8 g L−1 with these properties: a = 3 nm and DAB = 6.0 × 10−7 cm2 s−1. The solution viscosity is 1 cP. The hydrody- namic pressure on the protein side of the membrane is 20 pounds per square inch (psi) higher than on the filtrate side of the membrane. Determine the convective flow rate of the solution across the membrane and the rate at which the protein crosses the membrane. The solution on the feed side of the membrane is being stirred at 900 RPM.Why peripheral membrane proteins can be studied in absence of membrane and isolated under milder condition?Make a table with a scale of absorbance and the concentration of protein in Chromatin sample from the following data for excel graph Absorbance=660nm following data are of tubes with concern A =0 B=0.036 C=0.011 D=0.001 E=0.027 F=0.020 G=0.032 H1=0.176 H2=0.183 I1=0.150 I2=0.171 also plot the graph??
- You are interested in the mobility of two different unknown integral plasma membrane proteins—protein X and protein Y—in a cell. In one cell, you fluorescently label all the X proteins. In another cell, you label all the Y proteins. When you perform FRAP analysis on both cells, you find that most of the protein X fluorescence has recovered within 3 minutes, but recovery of the protein Y fluorescence is significantly slower. Even after 10 minutes, only 50% of the protein Y fluorescence has recovered. Describe the FRAP experimental protocol, explain what the results tell you about mobility of the X and Y proteins, and propose a possible explanation for why the mobilities of the two proteins differ.Certain cellular components appear to move bidirectionally on microtubules. Describe how this is possible given that microtubule orientation is fixed by the MTOC.Example Problem: FRAP Data Interpretation The diffusion rate of four different membrane proteins (A, B, C, and D) was measured using a FRAP experiment with purified liposomes. The FRAP recovery curves are shown below. Fluorescence intensity ROI A 3 Time Pre-bleaching Bleaching imaging imaging B Time Post-bleaching imaging C Time D Time (a) Which membrane protein exhibits the higher rate of diffusion in the lipid bilayer? A or B? C or D? (b) Explain the most likely cause of the difference in the recovery curves for proteins A and C.
- 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.Protein analysis by gel electrophoresis a). Using the gel image provided to calculate the electrophoretic relative mobility as a ratio of the distance of protein migration to the distance of the tracking dye migration (See Appendix B). If your dye front is not visible, measure the mobility relative to the bottom edge of the resolving gel. Include a labeled print-out of your gel image with your report. b). Plot log MW of the protein markers and commercial myoglobin vs. mobility. Determine the molecular weight of myoglobin obtained after the final purification step (Sample E) from the equation of the line. Submit a copy of your graph along with the gel image. c). Compare your sample E and commercial myoglobin with the ladder. Summary your results. order of sample (left to right) is : A B C D blank E blank Commercial Myoglobin Molecular LadderProtein transfer to a membrane from a developed electrophoretic gel can be performed under which of the following conditions?