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Updated: May 28, 2025
08:13
Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen
Published on: March 4, 2017
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Statistical Thermodynamics of the Protein Ensemble: Mediating Function and Evolution.
Vincent J Hilser1,2, James O Wrabl1, Charles E F Millard1,2
1Department of Biology, Johns Hopkins University, Baltimore, Maryland, USA;
Annual Review of Biophysics
|February 10, 2025
Summary
Nature selects for protein
Area of Science:
- Protein dynamics and evolution
- Biophysics
- Structural biology
Background:
- Proteins function through dynamic conformational fluctuations, not just static structures.
- Understanding how these dynamics evolve is crucial for protein adaptation.
Purpose of the Study:
- To investigate the role of local unfolding fluctuations in protein evolution.
- To determine if conformational equilibria are evolutionarily conserved.
- To develop methods for measuring and predicting these conserved energetics.
Main Methods:
- Review of studies on local unfolding fluctuations in native protein states.
- Analysis of adenylate kinase dynamics.
- Elucidation of thermodynamic principles governing protein energetics.
- Development of a quantitative probe for evolutionary conservation.
- Testing sequence compatibility for multiple protein folds.
Main Results:
- Local unfolding fluctuations are functionally important and ubiquitous in proteins.
- Thermodynamic principles reveal conserved protein energetics.
- These principles predict sequence compatibility across different protein folds.
- The locally unfolded ensemble is a key mechanism in protein evolution.
Conclusions:
- Protein evolution conserves not only ground states but also conformational equilibria.
- Thermodynamic insights provide a new perspective on protein adaptation and metamorphic proteins.
- The locally unfolded ensemble represents an emerging mechanism driving protein evolution.
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