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- 1E In terms of binding adenylate kinase, the Kd for ATP is ~50 M and the KI for GMP-PCP is ~50 nM. Explain how this may be possible in terms of molecular interactions. Name 4 different types of molecular interactions that may contribute to the increased binding affinity exhibited by GMP-PCP. Please help me in detailsWhich ONE of these statements is the most accurate definition of the mode of action of imatinib? Select one: A.It is a specific inhibitor of the BCR‐ABL1 fusion protein and blocks phosphatase activity by competing with adenosine triphosphate (ATP) binding B.It is a specific inhibitor of the BCR‐ABL1 fusion protein and blocks tyrosine kinase activity by competing with adenosine triphosphate (ATP) binding C.It is a specific inhibitor of the BCR‐ABL1 fusion protein and blocks tyrosine kinase activity by interaction with the enzyme site D.It is a specific inhibitor of the BCR‐ABL1 fusion protein and blocks phosphatase activity by interaction with the enzyme site2. The two diagrams to the right il- lustrate plots of steady-state ki- netic studies to characterize the in- teraction of heart muscle phos- phofructokinase-1 with a non-phy- siological, synthetic substrate fruc- tose-6-sulfate. Because the kcat is smaller than that for the natural 5 0.8- NH = 3.5 0.6- 0.4- 0.2- 10 μΜ 20 μΜ 48 µM substrate, higher enzyme concen- trations could be used. The results show the influence of increasing 2 0.2- 0.4- concentrations of ATP on the initial -0.6- > velocity of the enzyme catalyzed reaction in the presence of no -0.8F 4 12 20 28 36 44 52 60 68 76 84 92 .2 2.0 2.4 ΑMP () , 10 μΜ AMP (+ ) 20 μΜ AMP (-), and 48 µM AMP (-). [AΤP] (μΜ) log[ATP] (µM) (a) . Write the reaction in words catalyzed by the enzyme for the alternative substrate, describe how ATP interacts with the enzyme in the case of no AMP (•). (b) ! with respect to the binding of AMP and ATP to the allosteric effector sites on the enzyme. Explain the physical significance of the displacement…
- Two co-op students at your start-up company have been asked to evaluate the rate of reaction occurring in a transparent gel particle containing immobilized mouse melanoma cells. The equation for the reaction rate ris is: Vmax T'As Km+CAs where R=3.2 mm, Vmax= 0.12 gmol s' m3, CAS = 41 gmol m3, and Km=0.8 gmol m3. One student reports a reaction rate of 1.6x10 gmol st; the other reports 1.6x10 1º gmol s1. You left your calculator on the bus this morning, but must know quickly which student is correct. Use an order-of- magnitude calculation to identify the right answer. Which student is correct?4. a. Calculate the KM (Michaelis constant) and the vmax (the maximum initial rate) for both substrates (sphingosine and ATP). Show your work, and be careful about units. b. threo-dihydrosphingosine, a stereoisomer of sphingosine, is an inhibitor of sphingosine kinase. What kind of inhibitor (competitive, uncompetitive, noncompetitive) is threo-dihydrosphingosine? Citing information from the Lineweaver-Burke plots, explain how you can tell.Doxorubicin is a chemotherapeutic drug with an IC50 in MCF7 breast cancer cells of 0.01 microM. Assuming the cytotoxicity of doxorubicin follows 'classic' receptor theory what percentage of the cells will be viable following treatment of the cells with a concentration of doxorubicin of 0.01 microM? O 10% O 0.01% O 90% 50% 99.99%
- If intracellular [ATP] = 5 mM, [ADP] = 0.5 mM, and [Pi] = 1.0 mM, calculate the concentration of AMP at pH 7 and 25°C under the condition that the adenylate kinase reaction is at equilibrium.During an SAR effort to identify tyrosine kinase inhibitors, it was found that compound 2 was significantly more potent and selective than compound 1. To what might you attribute this improvement in activity and selectivity? Explain. IC-5 micromolar IC-0.1 mromolar2. The two diagrams to the right il- lustrate plots of steady-state ki- 5FA 0.8 netic studies to characterize the in- nH = 3.5 0.6- teraction of heart muscle phos- phofructokinase-1 with a non-phy- siological, synthetic substrate fruc- tose-6-sulfate. Because the kcat is 0.4- 0.2- smaller than that for the natural 10 μΜ 20 μΜ 48 μΜ substrate, higher enzyme concen- trations could be used. The results show the influence of increasing 0.2 0.4 concentrations of ATP on the initial -0.6- > velocity of the enzyme catalyzed reaction in the presence of no -0.8 4 12 20 28 36 44 52 60 68 76 84 92 1.2 2.0 2.4 AMP (•), 10 µM AMP (•), 20 µM AMP (-), and 48 µM AMP (). [ΑΤPΙ (μM) log[ATP] (µM) (а) how ATP interacts with the enzyme in the case of no AMP (•). Write the reaction in words catalyzed by the enzyme for the alternative substrate, describe (b) with respect to the binding of AMP and ATP to the allosteric effector sites on the enzyme. Explain the physical significance of the displacement of the…
- Based on your Lineweaver-Burk plot, what is the mode of PaESBL-1 inhibition by NSAMB? What is the equation for the double-reciprocal plot at 20 nMnM NAMB?1. Which expression below shows hemoglobin bound to a proton a. HbH+ b. HbO₂H+ c. HbBPG d. None of the above 2. Does hemoglobin, from you answer choice in question number 1, exist in the high affinity state or the low affinity state? What is hemoglobin's heterotropic ligand, based upon your answer choice in question number 1? 3. What type of the four catalysis reactions referenced in class is depicted by Asp52 in the diagram to the right? Mur2Ae H AcN H AcÑ Glu Foo Asp82 (1) HH CH₂OH Glu 00 ⁰0 Asp2 H НО OH Н GlcNAc CH₂OH H OH H H NAC First product2. The two diagrams to the right il- lustrate plots of steady-state ki- netic studies to characterize the in- FB 0.8- nH = 3.5 0.6- teraction of heart muscle phos- phofructokinase-1 with a non-phy- siological, synthetic substrate fruc- tose-6-sulfate. Because the kcat is smaller than that for the natural 0.4- 0.2- 10 μΜ 20 μΜ 48 μΜ substrate, higher enzyme concen- trations could be used. The results show the influence of increasing 2- 3.2- 0.4- concentrations of ATP on the initial -0.6- > velocity of the enzyme catalyzed reaction in the presence of no AMP (•), 10 µM AMP (•), 20 µM AMP (-), and 48 µM AMP (-). -0.8- 4 12 20 28 36 44 52 60 68 76 84 92 1.2 1.6 2.0 2.4 [AΤP (μΜ) log[ATP] (µM) (a) how ATP interacts with the enzyme in the case of no AMP (•). Write the reaction in words catalyzed by the enzyme for the alternative substrate, describe (b) with respect to the binding of AMP and ATP to the allosteric effector sites on the enzyme. Explain the physical significance of the…