2+The activity of the Ca 2+ -ATPase is regulated reversibly undernormal conditions to maintain homeostatic concentrations of Ca²-inside the sarcomere. However, in a rare genetic disorder, irreversibleactivation of the Ca 2+ -ATPase can occur. Assuming 37 °C,pH = 7.4, and the steadystate concentrations for ATP, ADP Pi,and Ca2+(out) given in part (a), calculate the minimum [Ca2+] insidea sarcomere that has irreversibly activated Ca 2+ -ATPase (i.e., theCa2+-ATPase activity is always “on”).Express your answer to two significant figures and include theappropriate units.

To calculate the minimum intracellular calcium concentration ([Ca2+] inside the sarcomere) when the…

Answered: 2+ The activity of the Ca 2+ -ATPase is…

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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Similar questions

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Begining with 1 M concentrations of each reactant and product at pH=7 and 25.0 degrees C, calculate the K'eq (to one decimal point) of the reaction Pyruvate + NADH+H+ <=> Lactate + NAD+.Note the temperature of this reaction will not affect the standard reducton potential delta E'o in the table 13-7b. please provide a comprehensive explanation with each step taken.
Explain the difference between ΔG°’ and ΔG and calculate the free energy (delta G) of hydrolysis of ATP in a rat liver cell in which the ATP, ADP, and Pi concentrations are 3.4, 1.3, and 4.8 mM.
Use the appropriate equation to calculate the free energy change for the movement of Nat into the depolarized nerve cell where the membrane potential is +50mV and the Nain/Naout ratio is 7.3/1. Assume the temperature is 37°C. Stop! For full credit: 1. Enter your answer in kJ, kilojoules. 2. Do not put units in the box. 3. Round your answer to the nearest tenth. If your calculator permits, do not round until the end for the sake of continuity. 4. If your answer is negative, include the sign and number with no space.
3L9
16c
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 table contains data about how different ASFV mutants affect enzyme activity-- for example the D29A mutant, where the D at position 29 was mutated to an A. Select three mutants at random, and for each mutant explain how that mutation could affect intermolecular force interactions (an example: hydrogen bonding could be disrupted by this mutation because…
3L6
In considering active transport by Na + -K + -ATPase at body temperature (37 o C), 3 Na+ are pumped out of the cell and 2 K + are pumped in for each ATP that is hydrolyzed to ADP + P i . Given that underyour experimental conditions, the DG for ATP hydrolysis is -10 kcal/mol, and that V is -60 mV, and that the pump maintains the internal Na + at 10mM, external Na + at 120 mM, internal K + at 120 mM and external K + at 8mM, what is the efficiency of the pump (i.e., what fraction of the energy available from ATP hydrolysis is required to drive transport at the provided levels)?
bo 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, Macmillan Leaming A 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]outside Choose 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 smaller positive number.
The enzyme mutase which is important for the synthetic of tyrosine and phenylalanine in saccharomyces cerevisiae has been studied as an example of an allosteric enzyme. Tyrosine acts as a negative effector for this enzyme. What effects would you see on the action of the enzyme were you to increase the concentration of tyrosine? The chorismate mutase would shift to its R conformation The curve showing the kinetics or chorismate mutase would shift to the right The curve showing the kinetics of chorismate mutase would shift to the left The chorismate mutase would become saturated more rapidly

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