bo Consider a uniport system where a carrier protein transports an uncharged substance A across a cell membrane. Suppose that ata certain ratio of [A] inside to [A] outside, the AG for the transport of substance A from outside the cell to the inside,Macmillan LeamingA outside → Ainside, is 10.7 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]outsideChoose the true statement about the transport of A under the conditions described.Because AG is positive, the ratio [A] inside/[A]outside must be less than one.Increasing [A]outside will cause AG for movement of Aoutside to Ainside to become a larger positive number.Movement of Ainside to Aoutside will be spontaneous.Decreasing the concentration of the uniport protein in the membrane will cause AG to become a smallerpositive number.

Answered: Image /qna-images/answer/ca287689-cdf9-4925-a3d2-2305db69c91d.jpg

Answered: bo Consider a uniport system where a…

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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Similar questions

Calculate ΔG°′ for the reaction A + B ⇌ C + D at 25°C when the equilibrium concentrations are [A] = 10 μM, [B] = 15 μM, [C] = 3 μM, and [D] = 5 μM. Is the reaction exergonic or endergonic under standard conditions?
© Macmillan Learning A outside → Ainside, is 10.9 kJ/mol at 25°C. 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, What is the ratio of the concentration of substance A inside the cell to the concentration outside? [A]inside [A] outside -81.28 Incorrect Answer Choose the true statement about the transport of A under the conditions described. Decreasing the concentration of the uniport protein in the membrane will cause AG to become a smaller positive number. Because AG is positive, the ratio [A] inside/[A] outside must be less than one. Increasing [A] outside will cause AG for movement of Aoutside to Ainside to become a larger positive number. Movement of Ainside to Aoutside will be spontaneous. Incorrect Answer
An antibody binds to another protein with anequilibrium constant, K, of 5 × 109 M–1. When it binds toa second, related protein, it forms three fewer hydrogenbonds, reducing its binding affinity by 11.9 kJ/mole. Whatis the K for its binding to the second protein? (Free-energychange is related to the equilibrium constant by the equa-tion ΔG° = –2.3 RT log K, where R is 8.3 × 10–3 kJ/(mole K)and T is 310 K.)
1. a. Calculate the physiological DG of the reaction shown below at 37°C, as it occurs in the cytosol ofneurons, with phosphocreatine at 4.7 mM, creatine at 1.0 mM, ADP at 0.73 mM, and ATP at 2.6mM. The standard free energy change for the overall reaction is –12.5 kJ/mol. Phosphocreatine + ADP ® creatine + ATP b. The enzyme phosphoglucomutase catalyzes the conversion of glucose 1-phosphate to glucose6-phosphate. Calculate the standard free energy change of this reaction if incubation of 20 mMglucose 1-phosphate (no glucose-6 phosphate initially present) yields a final equilibrium mixtureof 1.0 mM glucose 1-phosphate and 19 mM glucose 6-phosphate at 25°C and pH 7.0. c. If the rate of a nonenzymatic reaction is 1.2 x 10–2 μM s–1, what is the rate of the reaction at 37℃ inthe presence of an enzyme that reduces the activation energy by 30.5 kJ/mol?
What is the Keq of Reaction #3? Show your work & clearly label your answer. Is Reaction #3 favorable under mammalian cellular conditions when the concentration of dGTP is 0.2 M, dCMP is 20 mM, dGMP-dCMP is 7 mM, and PPi is 10 mM? Use △G to support your answer.
Given a matrix pH of 7.8 and an inner mitochondrial membrane pH of 7.06, calculate the Nernst potential across the IMM in a lizard cell that is 27 degrees C.
ver is given. A +B C+ D 1) Calculate AG for the above react un and indicáte whether the reaction is favorable or unfavorable [A] = 0.9 M 20°C AG° = 4 KJ/mol %3D [B] = 15mM [C] = 4mM [D] = 3 M R= 8.314 J/moleK %3D %3D 4.7 and explain how you know.
Heart and muscle cells, where myoglobin resides, maintains an intracellular pO2 of about 2.5 torr. Calculate the fractional saturation (for human myoglobin) if a small change (1 torr) in oxygen partial pressure occurs in either direction (ie what happens at 1.5 torr, what happens at 3.5 torr?) and explain how a small change in oxygen pressure dramatically changes the myoglobin oxygen binding.
In the situations described below, what is the free energy change if 1 mole of Na+ is transported across a membrane from a region where the concentration is 48 μM to a region where it is 110 mM? (Assume T=37∘C.) In the absence of a membrane potential.
3L9
A particular reaction has a ΔG‡ of 30.0 kJ mol-1 at 25.0 °C. In the presence of an enzyme, the same reaction has a ΔG‡ of 1.50 kJ mol-1 at the same temperature. Calculate the rate enhancement of this enzyme. (R = 8.3145 J mol-1 K-1)
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)

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