explain how ATP functions like a rechargeable battery, include the transfer of kinetic energy to potential energy in your explanation. also include where the energy that “charges” ETP comes from.
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- The relationship between ATP and ADP can be compared to the state of a battery. Which of the following statements best compares ATP,ADP and a battery?if an 8.4-oz (250 mL) energy drink can has 27 grams of sugar, calculate the moles of ATP produced in the body when 1 oz of the drink is consumed assuming all the sugars in 1 oz of the drink are composed of only glucose.As a result of an experiment following measurements were obtained from a cell: ATP concentration of 0.5 mM, ADP concentration of 0.1 mM, inorganic phosphate (Pi) concentration of 2 mM. Under these conditions calculate the actual free energy (AG) of the reaction of hydrolysis of ATP to ADP and Pi. (The standard energy (AG") of ATP = -31 kl/mol; RT = 2.58 kJ/mol) Select one: a. -28 kJ/mol b. -33 kJ/mol C. -42 kJ/mol d. -19 kJ/mol
- Use the Michaelis-Menten equation to complete the enzyme kinetic data set, when Km is known to have a value of 1 mmol/L. Upload your tabulated answers and show your calculations.As a result of an experiment following measurements were obtained from a cell: ATP concentration of 0.5 mM, ADP concentration of 0.1 mM, inorganic phosphate (Pi) concentration of 2 mM. Under these conditions calculate the actual free energy (AG) of the reaction of hydrolysis of ATP to ADP and Pi. (The standard energy (AG°) of ATP = -31 kJ/mol; RT = 2,58 kJ/mol) Select one: O a. -28 kJ/mol O b. -33 kJ/mol OC. -19 kJ/mol O d. -42 kJ/molConsider the following chemical reaction: Glucose + ATP → Glucose-6-Phosphate + ADP + Pi Given the following information, calculate the actual free energy change (G’) of this reaction. G’ of Glucose + ATP → Glucose-6-Phosphate + ADP + Pi = -16.7 kJ/mol [Glucose] = 5.0 mM [ATP] = 1.85 mM [Glucose-6-Phosphate] = 0.083 mM [ADP] = 0.14 mM [Pi] = 1.0 mM Temperature = 37 C R (Gas Constant) = 8.314 J/mol•K
- Below is kinetic data obtained for an enzyme-catalyzed reaction. The enzyme concentration is fixed at 100 nM. Using a Lineweaver-Burke plot, calculate the kcat value for this reaction. Report your answer to three significant figures in units of 1/sec.At different glucose concentrations (2 mol of glucose, 4 mol of glucose, 8 mol of glucose), at what time, in milliseconds, was the increase in ATP the greatest and how does this affect the potential (mV) graph? I am having hard time analyzing this thank youDetermine the direction that each of the reactions will progress. Assume that the reactants and products are present in equimolar amounts. The standard free energy of hydrolysis of ATP is - 30.5 kJ/mol. fructose + ATP fructose 6-phosphate + ADP The standard free energy of hydrolysis for fructose 6-phosphate is -15.9 kJ/mol. 3-phosphoglycerate + ATP 1,3-bisphosphoglycerate + ADP The standard free energy of hydrolysis for 1,3-bisphosphoglycerate is -49.3 kJ/mol. creatine + ATP creatine phosphate + ADP The standard free energy of hydrolysis for creatine phosphate is -43.0 kJ/mol.
- Define potential energy and kinetic energy and provide two specific examples of each. Explain how one form of energy can be converted into another. Will some energy be lost during this conversion? If so, what form will it take?Below is kinetic data obtained for an enzyme-catalyzed reaction. The enzyme concentration is fixed at 100 nM. Using a Lineweaver-Burke plot, calculate the Km value for this reaction. Report your answer to three significant figures in units of uM.Please handraw this graph with all the necessary detailed information: Imagine that I text enzyme rate for four different temperatures: 10 degrees celsius, 20 degrees celsisus, 30 degree celsius, and 40 degree celsius, in separate tubes. The enzyme appears to work faster as temperature increases, but completely ceases activity at 40 degrees celcius. Sketch a graph to show this outcome, but here you will graph product formation (nmoles/mL) vs. time (minutes). The graph should be 4 lines and HANDDRAWN. Include a legend if necessary. You do not need precise quantitivate values, but most show the correct trends on the graph.