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Updated: Jun 5, 2026

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
Published on: June 29, 2021
Applications of pressure perturbation calorimetry in biophysical studies
Yong Zhai1, Linus Okoro, Alan Cooper
1TU Dortmund University, Faculty of Chemistry - Biophysical Chemistry, Dortmund, Germany.
Abstract:
Pressure perturbation calorimetry (PPC) is a relatively new and efficient technique, to study the volumetric properties of biomolecules in solution. In PPC, the coefficient of thermal expansion of the partial volume of the biomolecule is deduced from the heat consumed or produced after small isothermal pressure jumps (typically±5 bar). This strongly depends on the interaction of the biomolecule with the solvent or cosolvent as well as on its packing and internal dynamic properties. This technique, complemented by ultrasound velocity and densitometry, provides valuable insight into the basic thermodynamic properties of solvation and volume effects accompanying phase transitions and interactions of biomolecular systems. Here we review data on protein folding, ligand binding processes, and phospholipid phase transitions, together with discussion of interpretation and further significant applications.
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