title: Probing volumetric properties of biomolecular systems by pressure perturbation calorimetry (PPC)--the effects of hydration, cosolvents and crowding.
abstract: Pressure perturbation calorimetry (PPC) is an 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. The expansion coefficient 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 with molecular acoustics and densimetry, provides valuable insights into the basic thermodynamic properties of solvation and volume effects accompanying interactions, reactions and phase transitions of biomolecular systems. After outlining the principles of the technique, we present representative examples on protein folding, including effects of cosolvents and crowding, together with a discussion of the interpretation, and further applications.
authors.affiliation: TU Dortmund University, Department of Chemistry and Chemical Biology, Physical Chemistry - Biophysical Chemistry, Otto-Hahn Str. 6, D-44227 Dortmund, Germany.
authors.forename: Saba
authors.initials: S
authors.lastname: Suladze
authors.affiliation: TU Dortmund University, Department of Chemistry and Chemical Biology, Physical Chemistry - Biophysical Chemistry, Otto-Hahn Str. 6, D-44227 Dortmund, Germany.
authors.forename: Marie
authors.initials: M
authors.lastname: Kahse
authors.affiliation: TU Dortmund University, Department of Chemistry and Chemical Biology, Physical Chemistry - Biophysical Chemistry, Otto-Hahn Str. 6, D-44227 Dortmund, Germany.
authors.forename: Nelli
authors.initials: N
authors.lastname: Erwin
authors.affiliation: TU Dortmund University, Department of Chemistry and Chemical Biology, Physical Chemistry - Biophysical Chemistry, Otto-Hahn Str. 6, D-44227 Dortmund, Germany.
authors.forename: Daniel
authors.initials: D
authors.lastname: Tomazic
authors.affiliation: TU Dortmund University, Department of Chemistry and Chemical Biology, Physical Chemistry - Biophysical Chemistry, Otto-Hahn Str. 6, D-44227 Dortmund, Germany. Electronic address: roland.winter@tu-dortmund.de.
authors.forename: Roland
authors.initials: R
authors.lastname: Winter
mesh_terms: D002151:Calorimetry / Q000379:methods*; D009113:Muramidase / Q000737:chemistry; D011137:Polystyrenes / Q000737:chemistry; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D012259:Ribonuclease, Pancreatic / Q000737:chemistry; D012997:Solvents / Q000737:chemistry; D013696:Temperature; D013816:Thermodynamics; D014867:Water / Q000737:chemistry
chemical_list: D011137:Polystyrenes; D011506:Proteins; D012997:Solvents; D014867:Water; D012259:Ribonuclease, Pancreatic; D009113:Muramidase
keywords: Cosolvents; Crowding; Lysozyme; Molecular acoustics; Pressure perturbation calorimetry; Protein folding