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- Utilising the provided class data generate the following graphs: I) Michaelis Menten; II) Lineweaver-Burk; and III) Hanes-Woolf. Ensure that you clearly label each graph,and add the relevant trendlines with equations. Table 1: Class data demonstrating the Absorbance at 700nm obtained for the alkaline phosphatase enzyme reaction Table 1 tube Abs700mm 1 0.000 2 0.060 2 0.090 4 0.140 5 0.190 6 0.250 7 0.290 The equipment we used are • 20mM Tris Buffer pH 8.5 • 33mM MgCl2 • Alkaline Phosphatase (2mg/ml) in 20mM Tris Buffer pH 8.5 • 4mM Glucose-1-phosphate • Acid Molybdate pH 5.0 • Reducing Agent • Distilled Water • Glass Test tubes • Tube Rack • Cuvette • Pipettes and Tips • Water bath set to 37oC The method we used is Method/Protocol: 1. Read the protocol in its entirety before starting. Take note of any additional information that appears in subsequent steps that may influence how previous steps are performed. 2. Using glass tubes, generate the reactions mixtures…Calculate the net charge on the following tripeptides at pH 5.0: (a) Leu-His-Asp [0] (b) Ala-Ile-Val [0] (c) Met-Lys-Arg [+2] (d) Which tripeptide will be retained the shortest on a cation-exchange chromatographic column in a pH 5.0 buffer? Why?pls explainWhy was absorbance measured at 420 nm in the enzyme kinetics experiment? To monitor thea. decrease in catechol concentrationb. increase in quinone concentrationc. decrease in polyphenol oxidase concentrationd. polyphenol oxidase-catechol complex concentrationLineweaver-Burk plot is the most used linearization method of the MichaelisMenten equation, but the main drawback is a/an:a. overemphasis to low substrate concentration and less emphasis to high substrate concentration.b. overemphasis to high substrate concentration and less emphasis to low substrate concentration.c. exaggeration to both ends of the reciprocal of the substrate concentration.d. lack of independent variables to x- and y- coordinates
- Protein: QQICIMFELTQISS Predict the products of the following reactions with the protein given, if there is none, write NO RXN. Also indicate, if the reaction is fast or slow.The ESI-MS spectrum in positive ionization mode for lysozyme is obtained. a. What is the molecular weight of the protein to 5 significant figures based on the two highlighted ion species? b. What is the charge of the peaks at 1101.5 and 1789.2.Consider the binding reaction L + R → LR, where L is a ligand and R is its receptor. When 1 × 10−3 M of L is added to a solution containing 5 × 10−2 M of R, 90 percent of the L binds to form LR. What is the Keq of this reaction? How will the Keq be affected by the addition of a protein that facilitates (catalyzes) this binding reaction? What is the dissociation equilibrium constant Kd?
- Given the following data, calculate Keq for the denaturation reaction of the protein β-lactoglobin at 25oC: ΔH° = –88 kJ/mol ΔS° = 0.3 kJ/mol. The free energy of hydrolysis of ATP in systems free of Mg2+ is −35.7 kJ/mol. When the concentration of this ion is 5 mM, ΔG°observed is approximately −31 kJ/mol at pH 7 and 38°C. Suggest a possible reason for this effect.Using the ActiveModel for phosphofructokinase (Trypanosoma), describe the difference between the APO1, AP02, and holoenzyme conformations.Legend: Blue – wild-type β-galactosidase Red – mutant β-galactosidase _________ a. What is the optimum pH of wild type β-galactosidase? _________ b. What is the optimum temperature of mutant β-galactosidase? _________ c. Which enzyme has the greater activity at pH 7.2? _________ d. Which enzyme has the greater activity at a temperature of 42.5oC? _________ e. Which enzyme has greater activity if pH decreases from 7.5 to 6.4? _________ f. Which enzyme has greater activity if temperature increases from 40oC to 41 oC?
- #1 Specify the role each of the following amino acids play within the crystal structure and/or active site for Be as specific as possible, with pictures (and mechanistic arrows) as necessary. His11 Arg140 Glu89 Trp68 #2 Provide a step-wise mechanism for the reaction Bisphosphoglycerate mutase catalyzes, using the amino acids responsible for aiding in catalysis. You do not need to add surrounding amino acids that aid in substrate specificity. (drawn out)Calculate the turnover number for an enzyme, assuming Vmax is 0.5 M.sec-1 and the concentration of the enzyme used is 0.002 M. Why is it useful to know this?a) Determine kcat (in units of sec-1) for a particular enzyme, given the following information: Vo = 144 mmol/min; [S] = 2 mM; Km = 0.5 mM; Enzyme Molecular weight = 40,000 mg/mmole; 8 mg of enzyme used in assay generating this data. b) In general, explain how the total enzyme concentration affects turnover number and Vmax?