1. Ifa Lineweaver-Burk plot gave a line with an equation of y=0.25 x +0.34, what are the values of KM and Vmax if the substrate concentration is in mM and the velocity in mM/s?
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- Plot a line weaver-burk graph for Km=6.30mM and Vmax=360uM/min when an experiment has 5 tubes with concentrations of substrates of 1.0mM, 10mM, 50mM, and 100mM.From the equation of a lineweaver-burke plot, calculate Km and Vmax. Show your work and include units. The equation is y=393.4x +8.4337The equation of the double reciprocal plot is y = 0.5294 x + 1.4960. What is the value of vmax (in M/s)? The substrate concentration is given in units of molarity (M) and reaction velocity has units of molarity per second (M/s). (Report to three significant figures)
- Consider the titration of 50.00 mL of 0.160 M NH3 with 0.200 M HCl. Calculate the pH at the following volumes of the titrant: VT = 0.00 (Initial Stage) VT = 20.00 VT = 30.00 VT = 40.00 (Equivalence Point Stage) VT = 45.00 Kb = 1.76 x 10-5What volume of a 40% v/v solution must be used to produce 500mL of 5% v/v solution?What is v/Vmax ratio when [S] = 4km? %3D
- You have measured the following data for enzyme X. Substrate Vo concentration (micromolar (mM) Isec) 0.05 10 0.1 60 0.5 175 1 250 350 490 10 492 20 494 50 499 100 498 200 498Ismail analyzed the triester content in an esterified oil using the gas chromatographic technique. The measurements for triester contents are 33.27, 33.37, and 33.34%. Calculate: (i) the average triester content (ii) the standard deviation, s for triester content (iii) the relative standard deviation for the triester contentSUBSTRATE CONCENTRATION [S] µM INITIAL VELOCITY V0 s-1 10 0.13 25 0.27 50 0.45 100 0.65 150 0.77 200 0.85 300 0.94 500 1.03 (i) a) Construct an empty table with the following column headings: Substrate concentration [S] and initial velocity (Vi) where [S] has the unit µM, and Vi has the unit mM/s. (ii) The table provided is the enzyme kinetic data for your mutated enzyme, whereby Vi was expressed using the unit ∆A(405 nm)/s. Using the standard curve, express Vi with the unit mM/s rather than ∆A(405 nm)/s. Place your answer in the table above alongside the appropriate [S]. Hint: To answer this question you need to use this standard curve equation=0.0419x (The slope of the line is= 0.0419) (iii) The unmutated form of your protein has a Km of 25 µM and a Vmax of 43 mM/s. The enzyme kinetic data for your enzyme with the amino acid substitution should now be displayed in the table above. Based on these data, what is Vmax? Km? and…
- You obtained the following raw data when setting up a Biuret standard curve: Absorbancy BSA (mg/ml) 540nm 0.158 1 0.210 0.260 0.305 0.360 0.410 0.455 7 0.510 0.530 0.550 10 0.554 What would the quality of the line-fit (R2 value) be if you do not exclude experimental outliers? (Give you answer to 4 decimal places) O-2N 34 56 o9An enzyme with concentration of 3.0 uM is added to a flask containing 125 uM of substrate. You know the Km is equal to 0.054 mM, and has a Vmax of 1.4 uM/s. What is the observed velocity? O 0.98 uM/s 0.074 uM/s O 5.2 um/s 1.4 uM/sTwo compounds with partition coefficients of 15 and 18 areto be separated on a column with Vm/Vs 3.0 and tm 1.0 min.Calculate the number of theoretical plates needed to produce aresolution of 1.5.