Please determine the template sequence used in a pyrosequencing reaction in the following graph. A 4G T 2G C 3T 4G 2T G CA G 2T 3 2 min 2 AG T CAG T C A G T C A G T C A G T C A G T C A G joud s'o
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- Define the following terms:a. amphibolic pathwayb. anaplerotic reactionc. glyoxylate cycled. reduction potentiale. conjugate redox pairCalculate 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?Consider the following equilibrium at 25ºC :Glucose-1-Phosphate Glucose-6-PhophateUsing the equilibrium concentrations of [Glucose-1-Phosphate] = 0.35 M and [Glucose-6-Phosphate] = 1.65 M, calculate BOTH K′eqand Gº′ for this reaction. Is this reaction exergonicor endergonic? R = 8.314 J/K·mol
- 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 actual, physiological ΔG for the reaction at 37 °C, as it occurs in the cytosol of neurons, with phosphocreatine at 4.7 mM, creatine at 1.0 mM, ADP at 0.73 mM, and ATP at 2.6 mM.A) Is this reaction ( in picture provided) in equilibrium? B) If it is not then ,what is ∆G' at 25°C if the concentration of Glucose-1-phosphate is 15.04µM and the concentration of Glucose-6-phosphate is 1.62 mM? Answer in Joules. Round to the correct number of significant figures. (There are 103 µM in 1mM.) Thank you so Much!!!
- 1. a. Calculate the physiological DG of the reaction shown below at 37°C, as it occurs in the cytosol ofneurons, with phosphocreatine at 4.7 mM, creatine at 1.0 mM, ADP at 0.73 mM, and ATP at 2.6mM. The standard free energy change for the overall reaction is –12.5 kJ/mol. Phosphocreatine + ADP ® creatine + ATP b. The enzyme phosphoglucomutase catalyzes the conversion of glucose 1-phosphate to glucose6-phosphate. Calculate the standard free energy change of this reaction if incubation of 20 mMglucose 1-phosphate (no glucose-6 phosphate initially present) yields a final equilibrium mixtureof 1.0 mM glucose 1-phosphate and 19 mM glucose 6-phosphate at 25°C and pH 7.0. c. If the rate of a nonenzymatic reaction is 1.2 x 10–2 μM s–1, what is the rate of the reaction at 37℃ inthe presence of an enzyme that reduces the activation energy by 30.5 kJ/mol?Calculate the overall ΔG° (report up to two decimal places) for the net reaction (see attached image). Answer: _____ kcal/mol Note: R = 1.98 x 10 -3 kcal/mol-KUsing Figure 1.3 of the Introduction as an example, a) draw all the structures of the tribasic amino acid lysine involved in the equilibrium reactions that would take place during titration against NaOH, starting with the fully protonated form below (draw the R-group in full). HAN+-CH- COOH (CH2)4 NH°+ b) indicate the numerical pa value of each equilibrium reaction, and which ionizable group is being dissociated in each step. c) indicate the net charge of the amino acid at each step and identify the zwitterion. d) Calculate the pI of this amino acid (show the calculation). e) What would be the predominant ionization states of this amino acid at physiological pH (7.4) and at this pH, what would the ratio of these two states be (show the calculation)?
- Beginning with the 1st tetrahedral intermediate, show the complete steps in chymotrypsin mechanism that occurs to form the 2nd chymotrypsin intermediate in the chymotrypsin active site. The substrate for chymotrypsin to be used is Ala-Tyr-Gly. Further, name the amino acid(s) that would be released as a result of the reactions you'd illustrated above.Write a balanced equation for each of the following reactions or reactionsequences.(a) The reaction catalyzed by PFK-2(b) The conversion of 2 moles of oxaloacetate to glucose(c) The conversion of glucose to UDP-Glc(d) The conversion of 2 moles of glycerol to glucose(e) The conversion of 2 moles of malate to glucose-6-phosphateWrite a balanced equation for each of the following reactions or reaction sequences. (a) The reaction catalyzed by PFK-2 (b) The conversion of 2 moles of oxaloacetate to glucose (c) The conversion of glucose to UDP-Glc (d) The conversion of 2 moles of glycerol toglucose (e) The conversion of 2 moles of malate to glucose-6-phosphate