Answer c and d thank u (c) To study molecular motors, scientists often use ATP analogs (molecules that look structurallylike ATP but have different chemical properties). One such molecule, AMPPNP, is shown below.How does this structure differ from ATP and how do you think this chemical difference willchange the behavior of an ATPase acitivty?но-р.P=0HO-P=ONHP-OHOHHO...(d) What state of the Na*K* pump would you expect to trap if you incubated the proteincomplex with the AMPPNP analog? Explain.

ATP or adenosine triphosphate is the energy currency of the cell.Molecular motors are machines that…

Answered: (c) To study molecular motors,…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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A 75 kg person doing light work requires about 3000 kcal of food energy perday, 40% of which is actually used by the body’s cells. (The other 60% is lostas heat and in waste products.) Before being used by the cells, effectively allof this energy is stored in ATP, which is then cleaved into ADP and PO3−2 , with the release of 12.5 kcal per mole of ATP.(a) How many moles of ATP are turned over per day in this fashion? Whatmass of ATP does this correspond to? (The molecular weight of ATP is507 g/mol.)(b) The body actually contains approximately 5 g ATP. Estimate the averagerecycle time for an ATP molecule. You see that it is much more efficientto reuse ADP rather than to synthesize it de novo (from scratch).
V-class proton pumps run backward relative to the F-class ATP synthase. Consider the cartoon, which shows the conformations of the beta-subunits and ATPIADP + Pj of the F-class synthase. Which of the following associations between the conformation of the beta subunit and ATP/ADP + P¡ is correct for V- Binding Change Mechanism loose binding ADP+P ATP ATP class pumps? C repeat ADP + P, ADP АТР tight binding АТР +P оpen АТР O The open conformation releases ATP. Hydrolysis of ATP to ADP + P¡ drives the change from tight to loose. O Binding of ADP + P¡ drives change from open to loose. Hydrolysis of ATP to ADP + Pj drives the change from open to loose.
The standard free energy of hydrolysis of inorganic polyphosphate (polyP) is about −20 kJ/mol for each Pi released. We calculated in Worked Example 13–2 that, in a cell, it takes about 50 kJ/mol of energy to synthesize ATPfrom ADP and Pi. Is it feasible for a cell to use polyphosphate to synthesize ATP from ADP? Explain your answer.
B) The actual concentrations of ATP, ADP and Pi differ by tissue/cell type (see table). Tissue/Cell Type ATP (mM) ADP (mM) Pi (mM) Liver 3.5 1.8 5.0 8.0 2.7 Skeletal Muscle 8.0 0.9 Brain 2.6 0.7 Calculate AG' for ATP hydrolysis in liver. (NOTE: assume 25°C and omit the concentration of water in your calculations).
The drug troglitazone was used to treat diabetes but was withdrawn from the market when patientswho took the drug suffered from severe side effects. The data below show the activity of an enzymein the steroid biosynthetic pathway in the presence and absence of 10 µM troglitazone.[S] (µM) v0 (pmol min-1)Create a plot of 1/v0 vs. 1/[S]. Calculate KM and vmax in presence and absence of inhibitor. Whattype of inhibitor is troglitazone? Clearly support your answer.
When a vertebrate dies, its muscles stiffen as they are deprived of ATP, a state called rigor mortis. Using your knowledge of the catalytic cycle ofmyosin in muscle contraction, explain the molecular basis of the rigor state.
In muscle cells, the AG for glucose+ATP2 glucose-6-P+ADP is –33.5 kJ•mol-'. In contrast, the AG for glucose – 6 – P fructose – 6 - P is –2.5 kJ · mol-1. (a) In a physiological context, which reaction is faster? How do you know? (b) The enzyme that catalyzes glucose + ATP 2 glucose important point of regulation in glycolysis, while the enzyme that catalyzes glucose – 6 – PZ fructose – 6 – P (phosphoglucose isomerase) is not. Why is hexokinase a good step at which to regulate glycolysis relative to phosphoglucose isomerase? 6 – P + ADP (hexokinase) is an | - |
Intracellular concentrations in resting muscle are as follows: fructose- 6-phosphate, 1.0 mM; fructose-1,6-bisphosphate, 10 mM; AMP, 0.1 mM; ADP, 0.5 mM; ATP, 5 mM; and P, 10 mM. Is the phosphofructokinase reac- tion in muscle more or less exergonic than under standard conditions? By how much?
A critical reaction in the production of energy to do work or drive chemical reactions in biological systems is the hydrolysis of adenosine triphosphate, ATP, to adenosine diphosphate, ADP, as described by the reaction ATP(aq)+H2O(l)⟶ADP(aq)+HPO2−4(aq)ATP(aq)+H2O(l)⟶ADP(aq)+HPO42−(aq) for which Δ?∘rxn=−30.5 kJ/molΔGrxn∘=−30.5 kJ/mol at 37.0 °C and pH 7.0. Calculate the value of Δ?rxnΔGrxn in a biological cell in which [ATP]=5.0 mM,[ATP]=5.0 mM, [ADP]=0.10 mM,[ADP]=0.10 mM, and [HPO2−4]=5.0 mM.[HPO42−]=5.0 mM. Δ?rxn=ΔGrxn= kJ/mol
a) (1) Calculate the physiological AG (not AG.) for the reaction: Phosphocreatine + ADP - creatine + ATP Given; Phosphocreatine + H;0 - creatine + Pi ADP + Pi → ATP + H;0 AG.' -43 kJ/mol AG.- +30.5 kJ/mol at 25°C as it occurs in the cytosol of neurons, in which phosphocreatine is present at 4.7 mM, creatine at 1.0 mM, ADP at 0.20 mM, and ATP at 2.6 mM. (R = 8.315 JK-' mol-) (ii) Caleulate the free energy change at standard conditions for the following reaction: Acetaldehyde + NADH + H* + Ethanol + NAD* The half- reactions are: Acetaldehyde + 2H + 2e + Ethanol E°- - 0.20V NAD-+ 2H- + 2e ++ NADH + H- E=-0.32V (F= 96.485 kJ/V/mol)
The phosphorylation of glucose to glucose 1-phosphate requires 5.0 kcal/mol of energy. This unfavorable reaction can be driven by the hydrolysis of ATP to ADP. (a) Write the equation for the coupled reaction. (b) How much energy is released in the coupled reaction? glucose + HPO4---------->2– glucose 1-phosphate + H2O
For each Pi released, the typical free energy of hydrolysis of inorganic polyphosphate (polyP) is about 20 kJ/mol. In Worked Example 13–2, we determined that synthesizing ATP from ADP and Pi requires roughly 50 kJ/mol of energy in a cell. Is it possible for a cell to manufacture ATP from ADP using polyphosphate? Give an explanation for your response.

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