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Related Concept Videos

Effects of Temperature on Free Energy02:11

Effects of Temperature on Free Energy

The spontaneity of a process depends upon the temperature of the system. Phase transitions, for example, will proceed spontaneously in one direction or the other depending upon the temperature of the substance in question. Likewise, some chemical reactions can also exhibit temperature-dependent spontaneities. To illustrate this concept, the equation relating free energy change to the enthalpy and entropy changes for the process is considered:
Fast Reactions01:27

Fast Reactions

Fast reactions occurring in times shorter than the time needed to mix reactants pose a unique challenge for investigation. In a liquid-phase continuous-flow system, reactants A and B are swiftly pushed into the mixing chamber, where mixing occurs within 1 ms. The reaction mixture then flows through an observation tube, and one measures light absorption to determine species concentrations at various points of the tube. This method is most appropriate when relatively large volumes of reactants...

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Related Experiment Video

Updated: Jul 7, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
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Published on: January 16, 2016

Computational analysis reveals temperature-induced stabilization of FAST-PETase.

Peter Stockinger1,2, Cornel Niederhauser2, Sebastien Farnaud1

  • 1Research Centre for Health & Life Sciences, Coventry University, Coventry CV1 5FB, United Kingdom.

Computational and Structural Biotechnology Journal
|March 28, 2025
PubMed
Summary

Machine learning engineered a PETase (FAST-PETase) for better plastic recycling. This variant shows increased stability at high temperatures due to unique conformational changes, aiding protein engineering efforts.

Keywords:
BiocatalysisEnzyme EngineeringMachine learningMolecular dynamicsPETPETasePlastics degradationThermostability

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How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project
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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

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Last Updated: Jul 7, 2026

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How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project
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11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

Area of Science:

  • Biotechnology
  • Enzyme Engineering
  • Computational Biology

Background:

  • Poly(ethyleneterephthalate) (PET) constitutes over 10% of global solid waste.
  • Wildtype PETases have limited activity and thermal stability for industrial plastic depolymerization.
  • FAST-PETase, engineered using machine learning, shows enhanced functionality, activity, stability, and tolerance.

Purpose of the Study:

  • To elucidate the molecular mechanisms behind FAST-PETase's improved thermal stability.
  • To compare the dynamics of wildtype IsPETase (WT-PETase) and FAST-PETase.
  • To identify thermolabile regions in WT-PETase and understand how mutations affect them.

Main Methods:

  • Comparative Constraint Network Analysis (CNAnalysis).
  • Molecular Dynamics (MD) simulations at 30°C and 50°C.
  • Physical energy calculations to determine the free energy of unfolding (ΔG(stability)).

Main Results:

  • Identified thermolabile sequence stretches in WT-PETase.
  • FAST-PETase mutations targeted these critical regions, reducing backbone flexibility at elevated temperatures.
  • In-silico and physical energy calculations indicated decreased free energy of unfolding and increased rigidity at higher temperatures for FAST-PETase.

Conclusions:

  • FAST-PETase achieves enhanced thermal stability through temperature-dependent conformational changes that rigidify the enzyme.
  • Findings provide insights into rational protein engineering for thermostability.
  • Contributes to understanding the thermal adaptation of thermophilic enzymes.