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The model I was given is picene and I need to answer this question:
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- Discuss the relationship of Lineweaver-Burke and Michaelis Menten equations. What are the importance of the double reciprocal plot, Michaelis constant, and Vmax?Pls help me with the given question and explain your correct answer, thank you A group of absent-minded scientists has two numbers (25.4 and 2.54) written on a scrap of paper. One scientists says: “I remember that one of these values was the standard deviation and the other the standard error of the mean, but I can’t remember which is which”. a)Which number is the standard deviation, and which is the standard error of the mean? b)What was the sample size? SE= s/√(2√n)Which parameters are plotted on the X and Y axes of a Kaplan-Meier graph?
- The extinction coefficient or absorptivity (ɛ) of protein A at 340 nm is 6440 M-1 cm-1, whereas protein B does not absorb at 340 nm. What absorbance will be observed when light at 340 nm passes through a 5 mm cuvette containing 10 µM of protein A and 10 µM of protein B? Beer-Lambert-law; A = ɛ x C x1; A = absorbance, C= concentration, 1= pathlength).What does the graph imply?Kwon Soon-young was asked by his CHEM 160.1 lab instructor to determine the isoelectric pH of an unknown protein sample which is said to be 20% histidine (pI = 7.59), 25% lysine (pI = 9.74), and 55% arginine (pI = 10.76). He plans to perform isoelectric precipitation in order to determine the IpH of the unknown protein sample. From the three buffer solutions below, at which particular buffer system do you think the unknown protein is most likely to precipitate? Explain your reasoning. BUFFER SYSTEM citrate buffer bicarbonate buffer methylamine-methylammonium chloride buffer pH 3.15 7.41 10.46
- 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 55Can you please explain why E is correct?Ok, thank you so much. In case of Km, we cant get the value? Do we just mention that 2.085 on x-axis will give the value for Km? Or have I misunderstood what you wrote
