disadvantage of using protein blast
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- Liposomes used in these vaccines contain some cationic lipids, or lipids with a positively charged head group. Explain why this is a sensible strategy for delivering genetic materials (or drugs) to a human cell.Explain the advantage of using Fluorescence Recovery After Photobleaching (FRAP) in determining protein localisation I notes = Notes Comments MAY 7.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%
- Help meTitration curve of an unknown amino acid The graph below shows a curve, which was obtained following titration of an unknown amino acid. Include a suitable descriptive title stating the identity of the unknown amino acid Use rectangles to precisely outline the regions in the graph where ionisable groups show buffering activity (base/acid ratio 1:10 to base/acid ratio 10:1); clearly associate the name of the ionisable group with the buffering regions; indicate within the graph all observable titration mid-points and all observable titration end-points and indicate estimates of the pKa of the three functional groups (do not provide pka values from the literature, you need to read the pka from the titration curve provided). Note that it is not possible to estimate the pka with more than one decimal precision due to limited resolution of the shown graph.Don't copy paste.
- Complementation and mapping analyse of Lac− mutantsNeed help, please. Answer choices are provided below for drop-down questions. 1. The overall charge of this protein at pH 7 is Drop-down answer choices are [positive, negative, or neutral] 2. In the first dimension of 2-D PAGE, this protein's isoelectric focusing point is Drop-down answer choices are [between 4 and 6, between 6 and 8, or between 8 and 10] 5. A mole of the above protein weighs ____ g. For 1 mL of a 4 mM solution of the above protein, you would need to weigh out ____ Drop-down answer choices are [g, mg, mcg, ng, or pg] (number and unit, at least one non-zero integer to the left of the decimal point, don't round)t, a The n of 4-19. In a common protein analysis, a dye binds to the protein and the color of the dye changes from brown to blue. The intensity of blue color is proportional to the amount of protein present. Protein (ug): 0.00 9.36 18.72 28.08 37.44 Absorbance: 0.466 0.676 0.883 1.086 1.280 2 (a) After subtracting the blank absorbance (0.466) from the remaining absorbances, use the method of least squares to determine the equation of the best straight line through these five points (n and intercept to express the equation in the form y (±s,) = [m (±sm)]x + [b (±sp)] with a reasonable number of signifi- cant figures. 02 5). Use the standard deviation of the slope and and (b) Make a graph showing the experimental data and the cal- culated straight line. and (c) An unknown gave an observed absorbance of 0.973. Cal- culate the number of micrograms of protein in the unknown, and estimate its uncertainty. nree
