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Related Concept Videos

Calculating the Equilibrium Constant02:46

Calculating the Equilibrium Constant

The equilibrium constant for a reaction is calculated from the equilibrium concentrations (or pressures) of its reactants and products. If these concentrations are known, the calculation simply involves their substitution into the Kc expression.
For example, gaseous nitrogen dioxide forms dinitrogen tetroxide according to this equation:
Calculating Equilibrium Concentrations02:05

Calculating Equilibrium Concentrations

Being able to calculate equilibrium concentrations is essential to many areas of science and technology—for example, in the formulation and dosing of pharmaceutical products. After a drug is ingested or injected, it is typically involved in several chemical equilibria that affect its ultimate concentration in the body system of interest. Knowledge of the quantitative aspects of these equilibria is required to compute a dosage amount that will solicit the desired therapeutic effect.
A more...
Calculating Standard Free Energy Changes02:49

Calculating Standard Free Energy Changes

The free energy change for a reaction that occurs under the standard conditions of 1 bar pressure and at 298 K is called the standard free energy change. Since free energy is a state function, its value depends only on the conditions of the initial and final states of the system. A convenient and common approach to the calculation of free energy changes for physical and chemical reactions is by use of widely available compilations of standard state thermodynamic data. One method involves the...
The Nernst Equation02:59

The Nernst Equation

Nonstandard Reaction Conditions
The interconnection between standard cell potentials and various thermodynamic parameters such as the standard free energy change ΔG° and equilibrium constant K has been previously explored. For example, a redox reaction involving zinc(II) and tin(II) ions at 1 M concentration with Eºcell = +0.291 V and ΔG° = −56.2 kJ is spontaneous.
Non-equilibrium in the Cell01:16

Non-equilibrium in the Cell

An important concept in studying metabolism and energy is that of chemical equilibrium. Most chemical reactions are reversible. They can proceed in both directions, releasing energy into their environment in one direction, and absorbing it from the environment in the other direction. The same is true for the chemical reactions involved in cell metabolism, such as the breaking down and building up of proteins into and from individual amino acids, respectively. Reactants within a closed system...
Thermodynamics: Activity Coefficient01:24

Thermodynamics: Activity Coefficient

Activity is the measure of the effective concentration of the species in solution. It can be expressed as the product of the molar concentration of the species and its activity coefficient. The activity coefficient is a dimensionless quantity and depends on the total ionic strength of the solution.
The activity coefficient is a measure of the deviation from ideal behavior. When the ionic strength of the solution is minimal, the activity coefficient of an ionic species is close to unity, making...

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Related Experiment Video

Updated: Jul 10, 2026

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions
13:00

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions

Published on: April 4, 2014

Computational thermostabilization of an enzyme.

Aaron Korkegian1, Margaret E Black, David Baker

  • 1Division of Basic Sciences, Fred Hutchinson Cancer Research Center (FHCRC), 1100 Fairview Avenue North, Seattle, WA 98109, USA.

Science (New York, N.Y.)
|May 10, 2005
PubMed
Summary

Computational methods rapidly identified three enzyme mutations. These mutations significantly increased thermostability and half-life without compromising catalytic efficiency, enabling enhanced bacterial growth.

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Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
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Measuring Enzymatic Stability by Isothermal Titration Calorimetry
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Measuring Enzymatic Stability by Isothermal Titration Calorimetry

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Related Experiment Videos

Last Updated: Jul 10, 2026

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions
13:00

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions

Published on: April 4, 2014

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
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Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability

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Measuring Enzymatic Stability by Isothermal Titration Calorimetry
08:37

Measuring Enzymatic Stability by Isothermal Titration Calorimetry

Published on: March 26, 2019

Area of Science:

  • Enzyme engineering
  • Computational biology
  • Metabolic engineering

Background:

  • Thermostabilizing enzymes for industrial applications is challenging using traditional methods.
  • Maintaining enzyme activity at elevated temperatures is crucial for many biotechnological processes.

Purpose of the Study:

  • To develop a rapid computational approach for enzyme thermostabilization.
  • To identify specific mutations that enhance enzyme stability and activity.
  • To demonstrate the coupled effect of molecular and metabolic engineering.

Main Methods:

  • Utilized a rapid computational strategy to identify mutations in a model enzyme.
  • Introduced three specific mutations into the enzyme.
  • Assessed changes in apparent melting temperature (Tm) and half-life at 50°C.
  • Evaluated enzyme's catalytic efficiency.
  • Measured bacterial growth rates under temperature-dependent conditions.

Main Results:

  • Identified three synergistic mutations that increased Tm by 10°C.
  • Achieved a 30-fold increase in enzyme half-life at 50°C.
  • Observed no reduction in the enzyme's catalytic efficiency.
  • Demonstrated an increased, temperature-dependent bacterial growth rate.

Conclusions:

  • A rapid computational approach can effectively engineer thermostable enzymes.
  • Synergistic mutations enhance enzyme stability and function.
  • Engineered enzymes can improve metabolic performance in a temperature-dependent manner.