In order to optimize acetylcholinesterase inhibition, a set of benzylamine derivatives were studied, and the following relationship was found: log) = -0.187 n+ 0.57o + 3.893
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- Methyl-labeled [14C]methionine at a specific activity of 2.0 millicuries per millimole was injected into rats. Six hours later the rats were killed. Phosphatidylcholine was isolated from the liver and found to have a specific activity of 1.5 millicuries per millimole. Calculate the proportions of phosphatidylcholine synthesized by the phosphatidylserine pathway and by the pathway starting from free choline. What further information would you need for your calculated values to reflect the true rates of these processes?For the following aspartate reaction in the presence of inhibitor, Km = 0.00065 M. Determine Vmax in both reactions and in the reaction without inhibitor, the Km. Identify whether the inhibition is competitive, non-competitive or uncompetitive. ( see attached picture ) how I and S bind to the E as shown by the Lineweaver Burk plot. the significance of the following obtained values for Km and Vmax. effect in slope and x-interceptHow was thermal stability measured in this paper and describe how GRL-1720 and 5h affect the thermal stability of Mpro and which drug has the larger effect? https://www.nature.com/articles/s41467-021-20900-6
- An experiment was carried out to measure the reaction rate of hydrolysis of acetylcholme (substrate) with serum enzymes (Eadie, 1949). In the experiment, two experiments were conducted, namely experiment 1 without using a prostigmine inhibitor and experiment 2 using a prostigmine inhibitor at 1.5 x 10^-7 mol/l. the data obtained are: a. Is prostigmine competitive or noncompetitive inhibitor? b. determine the value of km and rmax for the two experiments, compareIn a rat cardiomyocyte, the levels of creatine, phosphocreatine, and free phosphate were found to be 37.6mM, 40.3mM, and 8.02mM, respectively. Given that the standard free energy change is –43.0 kJ/mol, what is the true free energy change for phosphocreatine hydrolysis in the cardiomyocyte described above?Calculate, or make a best estimate of, the unknown factors in the situations listed in Table 1. Table 1. Data for problem 1. To find Data (i) Ek [K+]out = 4 mM; [K+]in = 130 mM (ii) [Cl-]in [Cl-]out = 570 mM; ECl = -65 mV (iii) ECl [Cl-]out = 150 mM; [Cl-]in = 8 mM; in a mammal (iv) [Na+]in Overshoot of action potential = +35 mV; saline [Na+] = 112 mM (v) [K+]in Blood [K+] = 3.2 mM; undershoot of action potential = -87 mV (vi) ECa [Ca2+]out = 5.6 mM; free [Ca2+]in = 0.8 mM (vii) [K+]out [K+]in = 350 mM; Ek = -82 mV
- The value of AG®' for the conversion of 3-phosphoglycerate to 2-phosphoglycerate (2PG) is +4.40 kJ/mol. If the concentration of 3-phosphoglycerate at equilibrium is 1.95 mM, what is the concentration of 2-phosphoglycerate? Assume a temperature of 25.0 °C. [2PG] = mMThe value of AH° for HBr(g) was first evaluated using the following standard enthalpy values obtained experimentally. Use these data to calculate the value of AHf° for HBr(g). Cl,(g)+2KB1(ag) – Br, (ag)+2KCI(ag) AH° =-96.2 kJ H,(g)+Cl, (g)- HCl(aq)+ KOH(aq) KC(aq)+H,O(!) 2HCI(g) AH° =-184 kJ AH° =-57.3 kJ HBr(aq)+ KOH(aq) KBr(aq)+ H,O(!) AH° =-57.3 kJ AH° =-77.0 kJ HC(g) Br,(g) HBr(g)- HCl(aq) disdlving in water Br, (aq) AH° =-4.2 kJ disolving in water HBr(aq) AH° =-79.9 kJ dissolving in water ΔΗΡ- i kJWhat is the concentration of B expressed in terms of A if the Kd is 33.0 uM, and the concentration of AB is 56.0 uM? A + B AB OB= 1850/A OB= 23 - A OB=23+ A OB= 0.589/A
- A Br selective electrode is applied for measuring bromide ions in saline solution. Cl' ions were found to interfere, with a kPot = 0.0050. %3D After calibration, the ISE equation was determined to be y = -70 mV - 59.2mV*log(x). If we measure a potential of 93 mV, and the [CI]=0.100 M, what was the [Br'] in units of M? O 0.00821 O 0.100 O 0.0050 O 0.123 O Correct answer not found in other optionsCalculate KI (in units of nmol L-1) for a competitive inhibitor that has α = 1.65 when 11.0 nmol L-1 inhibitor is present.The enzyme β-methylaspartase catalyzes the deamination of β-methylaspartate. For this aspartate reaction in the presence of the inhibitor hydroxymethylaspartate (3.8 M), determine KM and whether the inhibition is competitive or noncompetitive (KI = 1.0 M). [S], M V w/o inhibitor, M/s V w/ inhibitor, M/s 1x10-4 0.0259 0.0098 5x10-4 0.0917 0.040 1.5x10-3 0.136 0.086 2.5x10-3 0.150 0.120 5x10-3 0.165 0.142 In the ABSENCE of inhibitor: The Lineweaver-Burke equation is 1V=1V= __________ (1[S])(1[S]) + __________, and the KM is __________ M. In the PRESENCE of inhibitor: The Lineweaver-Burke equation is 1V=1V= ____________ (1[S])(1[S]) + ___________, and the KM is ___________ M. The type of inhibition is ____________. Round-off all answers to two (2) significant figures.