Journal
BIOPHYSICAL CHEMISTRY
Volume 156, Issue 1, Pages 13-23Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bpc.2010.12.010
Keywords
Pressure perturbation calorimetry; Protein folding; Ligand binding; Solvation; Cosolvents; alpha-lactalbumin; Phospholipids; Lipid phase transitions; Gramicidin; Cyclodextrin
Funding
- BMBF
- country Northrhine Westfalia
- European Union (Europaischer Fonds fur regionale Entwicklung)
- BBSRC (UK)
- Biotechnology and Biological Sciences Research Council [B20089] Funding Source: researchfish
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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 densitometty, 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. (C) 2011 Elsevier B.V. All rights reserved.
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