Consider a uniport system where a carrier protein transports an uncharged substance A across a cell membrane. Suppose that at a certain ratio of [A]inside to [A]outside, the AG for the transport of substance A from outside the cell to the inside, Aoutside → Ainside, is -12.1 kJ/mol at 25°C. What is the ratio of the concentration of substance A inside the cell to the concentration outside? [A]inside [A]outside 656275.63 Incorrect Choose the true statement about the transport of A under the conditions described. Increasing [A]outside will cause AG for movement of Aoutside to Ainside to become a smaller negative number. Decreasing the concentration of the uniport protein in the membrane will cause AG to become a larger negative number.

Consider a uniport system where a carrier protein transports an uncharged substance A across a cell membrane. Suppose that at a certain ratio of [A]inside to [A]outside, the AG for the transport of substance A from outside the cell to the inside, Aoutside → Ainside, is -12.1 kJ/mol at 25°C. What is the ratio of the concentration of substance A inside the cell to the concentration outside? [A]inside [A]outside 656275.63 Incorrect Choose the true statement about the transport of A under the conditions described. Increasing [A]outside will cause AG for movement of Aoutside to Ainside to become a smaller negative number. Decreasing the concentration of the uniport protein in the membrane will cause AG to become a larger negative number.

Human Physiology: From Cells to Systems (MindTap Course List)

9th Edition

ISBN:9781285866932

Author:Lauralee Sherwood

Publisher:Lauralee Sherwood

Chapter3: The Plasma Membrane And Membrane Potential

Section: Chapter Questions

Problem 1SQE: Using the Nernst equation, calculate the equilibrium potential for Ca2 and for C1 from the following...

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Consider a uniport system where a carrier protein transports an uncharged substance A across a cell membrane. Suppose that at a certain ratio of [A]inside to [A]outside, the AG for the transport of substance A from outside the cell to the inside, Aoutside → Ainside, is -11.3 kJ/mol at 25°C. What is the ratio of the concentration of substance A inside the cell to the concentration outside? [A]inside [A]outside = Choose the true statement about the transport of A under the conditions described. Increasing [A]outside will cause AG for movement of Aoutside to Ainside to become a smaller negative number. Decreasing the concentration of the uniport protein in the membrane will cause AG to become a larger negative number. Movement of Aoutside to Ainside will be spontaneous. Because AG is negative, the ratio [A]inside/[A]outside must be greater than one.
A one-to-one protein (P)-ligand (L) complexation (P + L PL) has a dissociation equilibrium constant (Kd) value of 100 nM at 25°C, and the Kd remains the same at 37°C. 1) What is AS of binding at 25°C? Assume ACp of the binding is 0 over the temperature range. AS = 1.34E2 kJ/(mol*K) (note the unit!!) (sig. fig =3) 2) What is the concentration of the PL complex formed at equilibrium when you mix 0.20 uM (microM) of Protein and 1.0 uM of Ligand together at 37°C? PL at equilibrium = 8.1E-1 uM (note the unit!!) (sig. fig =2)
The effect of temperature on the hydrolysis of lactose by a ß-galactosidase is shown below in Table 1. The temperature coefficient, Q10 is the factor by which the rate increases by raising the temperature 10°C. The universal gas constant, R is 8.314 J/mol.K. (a) (b) Table 1: Data of Vmax over temperature T (°C) 20 30 35 40 45 Vmax (umoles/min.mg protein) 4.50 8.65 11.80 15.96 21.36 Plot the graph of In Vm vs 1/T using any spreadsheet software (include all appropriate labels and equation). Calculate the activation energy Ea and temperature coefficient Q10.
The acidity of the stomach is maintained by the H*/K* ATPase in parietal cells of the gastric mucosa. These cells have an internal pH = 7.4. The H*/K* ATPase transports H* across the cellular membrane into the stomach where pH = 0.8. (a) Given a membrane potential of 65 mV (inside negative), calculate AG in kJ/mol for the transport of H* into the stomach at 37 °C. Show your work. (b) The hydrolysis of ATP is directly coupled to H* transport and the stoichiometry of the transport reaction is such that 1 mol of ATP is hydrolyzed for every 1 mol of H* transported into the stomach. ATP is hydrolyzed by the ATPase on the inside of the cell. Under the conditions given in part (a) and assuming the steady-state concentrations of ATP, ADP and P₁ given below, is the transport of H* in to the stomach thermodynamically favorable at 37 °C? Show the calculation that supports your answer. Steady-state intracellular concentrations: ATP = 4.2 mM ADP = 360 μM Pi = 5.4 mM For ATP hydrolysis at 37 °C: ATP…
A bacterial enzyme catalyzes the hydrolysis of maltose as shown in the reaction given below: Maltose + H2O -> 2 glucose If the reaction has a Km of 0.135 mM and a V max of 65 m mol/min. What is the reaction velocity when the concentration of maltose is 1.0 mM?
Neutral sphingomyelinase 2 converts sphingomyelin into ceramide and phosphorcholine. What kind of enzyme is it? Assume Vmax is 35 µM min-1. When you provide 3.0 x 10-5 M of sphingomyelin, you observe an initial velocity of 6.0 µM min-1. Calculate the KM.
A bacterial enzyme catalyzes the hydrolysis of maltose as shown in the reaction given below: Maltose + H2O -> 2 glucose If the reaction has a Km of 0.135 mM and a V max of 65 umol/min. What is the reaction velocity when the concentration of maltose is 1.0 mM? (Please take note of the units)
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, compare
Consider a suspension of particles (isoelectric point is at pH 6) in water at pH 2 and a NaCl concentration of 0.001 M. Describe how the strength of repulsion varies with the following changes, assuming all other conditions remain constant. Give a description (more than just increase or decrease) in terms of the effect on the double layer thickness and the zeta potential. (a) Change from 0.001 M NaCl to 0.1 M NaCl, (b) Change from pH = 2 to pH = 5.
An enzyme has the following values: vmax's; 0.028 M s-' and 0.021 M s-' (I), and km's; 0.00198 M and 0.00197 M (I), when the total concentration of enzyme is 10-º M. The (I) values were determined with 1 microM inhibitor. Select the value closest to the k, for this enzyme. (hint 1 microM = 10-6 M).
The equation of the double reciprocal plot is y = 0.5294 x + 1.4960. What is the value of vmax (in M/s)? The substrate concentration is given in units of molarity (M) and reaction velocity has units of molarity per second (M/s). (Report to three significant figures)
ΔG°′ for the isomerization reaction glucose-1-phosphate (G1P) ⇌ glucose-6-phosphate (G6P) is −7.1 kJ · mol−1. Calculate the equilibrium ratio of [G1P] to [G6P] at 25°C.