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Related Concept Videos

Le Chatelier's Principle: Changing Temperature02:19

Le Chatelier's Principle: Changing Temperature

Consistent with the law of mass action, an equilibrium stressed by a change in concentration will shift to re-establish equilibrium without any change in the value of the equilibrium constant, K. When an equilibrium shifts in response to a temperature change, however, it is re-established with a different relative composition that exhibits a different value for the equilibrium constant.
To understand this phenomenon, consider the elementary reaction:
Third Law of Thermodynamics02:38

Third Law of Thermodynamics

A pure, perfectly crystalline solid possessing no kinetic energy (that is, at a temperature of absolute zero, 0 K) may be described by a single microstate, as its purity, perfect crystallinity,and complete lack of motion means there is but one possible location for each identical atom or molecule comprising the crystal (W = 1). According to the Boltzmann equation, the entropy of this system is zero.
Standard Entropy Change for a Reaction03:00

Standard Entropy Change for a Reaction

Entropy is a state function, so the standard entropy change for a chemical reaction (ΔS°rxn) can be calculated from the difference in standard entropy between the products and the reactants.
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The Equilibrium Binding Constant and Binding Strength

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The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
Chemical Equilibria: Redefining Equilibrium Constant01:20

Chemical Equilibria: Redefining Equilibrium Constant

The effect of an inert salt on the solubility of a sparingly soluble salt is known as the salt effect. The degree of the salt effect varies with the ionic strength of the solution, which in turn depends on the activity of the species in the solution. The activity is expressed as the product of concentration and the activity coefficient of the species.
To calculate the equilibrium constants of solutions of moderately high ionic strength, one must account for the salt effect. This redefined...

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Related Experiment Video

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Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
08:58

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Geometric programming, chemical equilibrium, and the anti-entropy function.

R J Duffin1, C Zener

  • 1CARNEGIE-MELLON UNIVERSITY, PITTSBURGH, PENNSYLVANIA.

Proceedings of the National Academy of Sciences of the United States of America
|July 1, 1969
PubMed
Summary

This study introduces a duality principle in thermodynamics, stating maximum entropy equals minimum anti-entropy. This principle simplifies calculating chemical equilibrium concentrations by minimizing an anti-Helmholtz function.

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Area of Science:

  • Thermodynamics
  • Chemical Equilibrium
  • Geometric Programming

Background:

  • Classical thermodynamics characterizes equilibrium by maximizing entropy (S).
  • This approach involves maximizing S with respect to extensive variables under constraints.
  • An alternative characterization of equilibrium is needed for simplified calculations.

Purpose of the Study:

  • To introduce and apply a duality principle in thermodynamics.
  • To demonstrate a new method for calculating chemical equilibrium.
  • To simplify the process of determining equilibrium concentrations.

Main Methods:

  • Formulating a duality principle: maximum S = minimum S(*).
  • Applying the principle to chemical equilibrium, leading to minimum Helmholtz free energy (F) = maximum anti-Helmholtz function (F(*)).
  • Proving the principle using the duality theorem of geometric programming.

Main Results:

  • Established a duality principle for thermodynamics: maximum entropy (S) equals minimum anti-entropy (S(*)).
  • Demonstrated that chemical equilibrium can be characterized by minimizing the anti-Helmholtz function (F(*)).
  • Showcased an unconstrained maximization problem for F(*) simplifying equilibrium concentration calculations.

Conclusions:

  • The duality principle offers a novel perspective on thermodynamic equilibrium.
  • Minimizing the anti-Helmholtz function provides a practical method for determining equilibrium concentrations.
  • Geometric programming's duality theorem validates this thermodynamic approach.