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Related Concept Videos

Predicting Reaction Outcomes02:24

Predicting Reaction Outcomes

Kinetics describes the rate and path by which a reaction occurs. In contrast, thermodynamics deals with state functions and describes the properties, behavior, and components of a system. It is not concerned with the path taken by the process and cannot address the rate at which a reaction occurs. Although it does provide information about what can happen during a reaction process, it does not describe the detailed steps of what appears on an atomic or a molecular level. On the other hand,...
Transition State Theory01:25

Transition State Theory

Transition-state theory, also known as activated-complex theory, provides a molecular-level explanation of reaction rates in both gas-phase and solution-phase reactions. It extends earlier kinetic models by considering the formation of a short-lived, high-energy configuration during a reaction.The progress of a chemical reaction can be represented using a reaction profile, which plots potential energy against the reaction coordinate. As two reactant molecules approach one another, their...
Reversible or Opposing Reactions01:26

Reversible or Opposing Reactions

Reversible or opposing reactions play a crucial role in understanding the dynamic nature of chemical processes. While kinetics focuses on how reactions proceed, thermodynamics emphasizes that most reactions do not reach completion. Instead, a reverse reaction starts occurring over time, and when its rate equals that of the forward reaction, a dynamic equilibrium is established.For example, consider a simple chemical process where A forms B reversibly. The rate constants for the forward and...
Temperature Dependence on Reaction Rate02:55

Temperature Dependence on Reaction Rate

The Collision Theory
Atoms, molecules, or ions must collide before they can react with each other. Atoms must be close together to form chemical bonds. This premise is the basis for a theory that explains many observations regarding chemical kinetics, including factors affecting reaction rates.
The collision theory is based on the postulates that (i) the reaction rate is proportional to the rate of reactant collisions, (ii) the reacting species collide in an orientation allowing contact between...
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:
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:

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Related Experiment Video

Updated: May 31, 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

Better biomolecule thermodynamics from kinetics.

Kiran Girdhar1, Gregory Scott, Yann R Chemla

  • 1Center for Biophysics and Computational Biology, University of Illinois, Urbana, Illinois 61801, USA.

The Journal of Chemical Physics
|July 13, 2011
PubMed
Summary

This study introduces a kinetics-based method to accurately measure protein stability by eliminating problematic denaturation curve baselines. This approach reliably extracts thermodynamic data, even for complex protein folding scenarios.

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Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
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Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

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Related Experiment Videos

Last Updated: May 31, 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

Measuring Biomolecular DSC Profiles with Thermolabile Ligands to Rapidly Characterize Folding and Binding Interactions
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Measuring Biomolecular DSC Profiles with Thermolabile Ligands to Rapidly Characterize Folding and Binding Interactions

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Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

Area of Science:

  • Biophysics
  • Protein Chemistry
  • Biochemistry

Background:

  • Protein stability is crucial for function and is typically measured using denaturation curves.
  • Denaturation curves can be complicated by nonlinear, steep, or incomplete baselines, hindering accurate thermodynamic characterization.
  • These baselines arise from chromophore sensitivity to solvent conditions, structural evolution within thermodynamic states, or low folding barriers.

Purpose of the Study:

  • To develop a method that overcomes limitations of traditional denaturation curves by utilizing kinetics.
  • To accurately extract protein unfolding thermodynamics by eliminating baseline artifacts.
  • To provide a reliable approach for characterizing protein stability, particularly in challenging cases.

Main Methods:

  • Leveraging the time scale separation between fast intra-state relaxation and slower inter-state transitions.
  • Deriving simple formulas to extract thermodynamic parameters from kinetic data.
  • Applying the "thermodynamics from kinetics" approach to model data and experimental cases.

Main Results:

  • Kinetics effectively eliminates baseline issues by separating fast relaxation processes from slow population switching.
  • The derived formulas enable reliable extraction of unfolding thermodynamics.
  • The method successfully determined the melting temperature (T(m)) for the PI3K SH3 domain, a protein known for unreliable conventional fitting.

Conclusions:

  • The "thermodynamics from kinetics" approach offers a robust solution for analyzing protein denaturation.
  • This method enhances the reliability of protein stability measurements, especially for proteins exhibiting complex denaturation profiles.
  • Accurate thermodynamic characterization is achievable even when conventional fitting methods fail.