W) Plot the "specific fluorescence” against time in a graph, and comment on the result.
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HEEELP -ME with this exersice please.
I dont understand which values I should use for plotting the graph
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- pls explain Increasing the saturation of the ammonium sulfate is a prerequisite in isolating a target protein that is rich in Cys and Tyr residues. Which of the following techniques should be considered in accurately quantifying the isolated protein?I. Running the isolated protein in a dialysis or GFC set up.II. Using Biuret or BCA assay as the colorimetric quantitation method.III. Using Bradford or Lowry assay as the colorimetric quantitation method.A. I onlyB. II onlyC. I and IIID. I, II and III. Bradford Assay is most suitable to use when the extraction buffer is below the target protein’s pI. This is so because the protein would be morea. Positively charged allowing the CBB G-250 dye to bind via its sulfonate groups.b. Negatively charged allowing the CBB G-250 dye to bind via its sulfonate groups.c. Neutrally charged allowing the CBB G-250 dye to bind via its sulfonate groups.d. Zwitterionic allowing the CBB G-250 dye to bind via its sulfonate groups.The movements of single motor-protein moleculescan be analyzed directly. Using polarized laser light, it ispossible to create interference patterns that exert a cen-trally directed force, ranging from zero at the center to afew piconewtons at the periphery (about 200 nm from thecenter). Individual molecules that enter the interferencepattern are rapidly pushed to the center, allowing them tobe captured and moved at the experimenter’s discretion.Using such “optical tweezers,” single kinesin mol-ecules can be positioned on a microtubule that is fixed toa coverslip. Although a single kinesin molecule cannotbe seen optically, it can be tagged with a silica bead andtracked indirectly by following the bead (Figure Q16–3A).In the absence of ATP, the kinesin molecule remains at thecenter of the interference pattern, but with ATP it movestoward the plus end of the microtubule. As kinesin movesalong the microtubule, it encounters the force of the inter-ference pattern, which simulates the load…Beer's Law to determine Protein Concentration You have purified a recombinant form of the p53 protein from E. coli and determined the A280 to be1.35. Calculate the molar and mass concentration of the purified protein if the extinction coefficientand molecular weight of p53 is 35,410 M-1 cm-1 and 43,653 Da, respectively (l = 1 cm).
- In Multi-Column Purification of rGFP. What happens to the protein amount, protein purity, and/or specific activity of a purification fraction if one of the three is changed? (i.e. understand the relationship between the three.)Pls explain If the voltage were NOT increased at the start of the resolving gel run, the overall experiment time will ______, while the calculated electrophoretic mobilities will ______.a. increase, increaseb. increase, decreasec. decrease, increased. decrease, decreasePick all that are TRUE regarding analysis of quaternary structures of proteins using polyacrylamide electrophoresis:I. The added β-mercaptoethanol disrupts S--S bonds bridging the polypeptide chains causing the appearance of higher Rf bands compared to the native protein run. II. Heating up any protein before subjecting to SDS-PAGE will always result in the formation of more than one band.III. A good asymmetrical gel layout would be : (Lane 1) MW ladder, (2) native protein, (3) protein + β-ME, (4) protein + HCL, (5) protein + β-ME + HCl.IV. Formation of a single band in the protein + β-ME + HCl run, whose Rf is lower than the native run, could be indicative that the protein is a homodimer.A. I onlyB. I and IIC. II and…Fluorescence-activated cell sorting (FACS) is a powerful technique for separating cells according to their content of particular molecules. For example, a fluorescence-labeled antibody specific for a cell-surface protein can be used to detect cells containing such a molecule. Suppose that you want to isolate cells that possess a receptor enabling them to detect bacterial degradation products. However, you do not yet have an antibody directed against this receptor. Which fluorescence-labeled molecule would you prepare to identify such cells?
- Using the pKa data in as shown and the Henderson-Hasselbalch equation,calculate the approximate net charge on each of the four common ribonucleoside 5′-monophosphates (rNMPs) at pH 3.8. If a mixture of these rNMPs was placed in an electrophoresis apparatus, as shown, draw four bands to predict the direction and relative migration rate of each.b. Compounds A, B, C, and D are known to be intermediates in the pathway for production of protein E. To determine where the block in protein-E production occurred in each individual, the various intermediates were given to each individuals cel Is in culture. After a few weeks of growth with the intermediate, the cells were assayed for the production of protein E. The results for each individuals cells are given in the following table. A plus sign means that protein E was produced after the cells were given the intermediate listed at the top of the column. A minus sign means that the cells still could not produce protein E even after being exposed to the intermediate at the top of the column. Denote the point in the pathway in which each individual is blocked.a. Compounds A, B, C, and D are known to be intermediates in the pathway for production of protein E. To determine where the block in protein-E production occurred in each individual, the various intermediates were given to each individuals cel Is in culture. After a few weeks of growth with the intermediate, the cells were assayed for the production of protein E. The results for each individuals cells are given in the following table. A plus sign means that protein E was produced after the cells were given the intermediate listed at the top of the column. A minus sign means that the cells still could not produce protein E even after being exposed to the intermediate at the top of the column. Draw the pathway leading to the production of protein E.
- A chain of biochemical events is responsible for Aequorea victoria turning green. Firstly, the protein aequorin converts chemical energy into blue light. A second protein, known as GFP (green fluorescent protein), absorbs the light. Aequorin is a 21 kDa protein with a pI of 4.5 that generates blue light from an attached non-protein chromophore. GFP is a 27 kDa protein with a pI of 6.2. In order for it to fluoresce, 3 amino acids undergo a remarkable reaction when they are folded in the right way. Aequorin does not absorb light in the visible range, and GFP absorbs light at 395 nm and 475 nm. 1. Sketch what you would see if you ran a mixture of aequorin and GFP over a size-exclusion column. In your sketch, include absorbance data at 280, 395, and 475 nm.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??In a pUC19 digest for 1 ug of pUC19 (DNA conc. 282ng/ul) using 10X Cutsmart buffer, pure water and BamHI enzyme in a total volume of 40 ul, how much of each solution is added to the total volume?