Two different proteins X andY are dissolved in aqueous solution at 37 °C. The proteins bind in a 1:1 ratio to form XY.A solution that is initially 1.00 mM in each protein is allowed to reach equilibrium. At equilibrium, 0.15 mM of free X and 0.15 mM of free Y remain.
Two different proteins X andY are dissolved in aqueous solution at 37 °C. The proteins bind in a 1:1 ratio to form XY.A solution that is initially 1.00 mM in each protein is allowed to reach equilibrium. At equilibrium, 0.15 mM of free X and 0.15 mM of free Y remain.
Chemistry
10th Edition
ISBN:9781305957404
Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Chapter1: Chemical Foundations
Section: Chapter Questions
Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...
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Transcribed Image Text:**Equilibrium Binding of Proteins X and Y**
Two different proteins, X and Y, are dissolved in an aqueous solution at 37°C. These proteins bind together in a 1:1 ratio to form the complex XY. Initially, the solution contains each protein at a concentration of 1.00 mM. The reaction is allowed to reach equilibrium. At this point, the solution contains 0.15 mM of free X and 0.15 mM of free Y.
This indicates that most of the proteins have formed the complex XY at equilibrium, with a much smaller concentration of unbound proteins remaining in the solution. This demonstrates the binding affinity between the proteins under the given conditions.
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