Applications of pressure perturbation calorimetry in biophysical studies

Yong, Z., Okoro, L., Cooper, A. and Winter, R. (2011) Applications of pressure perturbation calorimetry in biophysical studies. Biophysical Chemistry, 156(1), pp. 13-23. (doi: 10.1016/j.bpc.2010.12.010)

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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 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.

Item Type:Articles
Keywords:Pressure perturbation calorimetry, protein folding, ligand binding, solvation, cosolvents, α-lactalbumin, phospholipids, lipid phase transitions, gramicidin, cyclodextrin
Glasgow Author(s) Enlighten ID:Cooper, Professor Alan
Authors: Yong, Z., Okoro, L., Cooper, A., and Winter, R.
Subjects:Q Science > QD Chemistry
College/School:College of Science and Engineering > School of Chemistry
Journal Name:Biophysical Chemistry
Publisher:Elsevier BV
ISSN (Online):1873-4200
Published Online:01 January 2011
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