What is Kc for the reaction? **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.

Equilibrium constant is the ratio of product of concentration of product raised stoichiometry…

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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Question

What is Kc for the reaction?

**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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