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Related Concept Videos

Thermodynamic Potentials01:26

Thermodynamic Potentials

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Thermodynamic potentials are state functions that are extremely useful in analyzing a thermodynamic system. They have dimensions of energy. The four important thermodynamic potentials are internal energy, enthalpy, Helmholtz free energy, and Gibbs free energy. These thermodynamic potentials can be expressed using two of the following variables: pressure, volume, temperature, and entropy. These two variables are expressed as the rate of change of the thermodynamic potential with respect to other...
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Maxwell's thermodynamic relations are very useful in solving problems in thermodynamics. Each of Maxwell's relations relates a partial differential between quantities that can be hard to measure experimentally to a partial differential between quantities that can be easily measured. These relations are a set of equations derivable from the symmetry of the second derivatives and the thermodynamic potentials.
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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...
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Related Experiment Video

Updated: Jun 14, 2025

Measuring Biomolecular DSC Profiles with Thermolabile Ligands to Rapidly Characterize Folding and Binding Interactions
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TPPU_DSF: A Web Application to Calculate Thermodynamic Parameters Using DSF Data.

Pau Martin-Malpartida1, Carles Torner1, Aurora Martinez2

  • 1Institute for Research in Biomedicine, The Barcelona Institute of Science and Technology (BIST), Baldiri Reixac, 10, Barcelona 08028, Spain.

Journal of Molecular Biology
|September 5, 2024
PubMed
Summary
This summary is machine-generated.

TPPU_DSF is a free web application that automates the analysis of differential scanning fluorimetry (DSF) data. It calculates thermodynamic parameters for protein unfolding, improving hit detection in screening and reducing assay costs.

Keywords:
Differential scanning fluorimetryhigh-throughput compound screeninghit selection, hit ratethermal shift assaythermodynamic parameters

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Differential Scanning Fluorimetry (DSF) is widely used to study protein thermal stability.
  • Analysis of DSF data often relies on melting temperature (Tm) shifts, which can be insufficient for hit detection.
  • Calculating thermodynamic parameters offers a more comprehensive understanding of protein stability and ligand interactions.

Purpose of the Study:

  • To introduce TPPU_DSF, a novel, free, and open-source web application.
  • To automate the analysis of protein unfolding data obtained from DSF experiments.
  • To enable the calculation of thermodynamic parameters from DSF data.

Main Methods:

  • Development of a web application, TPPU_DSF.
  • Implementation of automated data processing for DSF experiments.
  • Calculation of thermodynamic parameters, including changes in Gibbs free energy of unfolding (ΔGu°).

Main Results:

  • TPPU_DSF successfully opens, converts, fits, and calculates thermodynamic parameters from standard DSF data.
  • The application automates the analysis process, saving time and resources.
  • Thermodynamic parameters provide a more robust method for hit identification in compound screening compared to Tm alone.

Conclusions:

  • TPPU_DSF enhances the utility of DSF by providing automated thermodynamic analysis.
  • The software improves the accuracy and efficiency of identifying protein binders in screening campaigns.
  • TPPU_DSF aids in optimizing protein constructs and buffer conditions by incorporating thermodynamic insights.