Literature DB >> 21255903

Applications of pressure perturbation calorimetry in biophysical studies.

Yong Zhai1, Linus Okoro, Alan Cooper, Roland Winter.   

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.
Copyright © 2011 Elsevier B.V. All rights reserved.

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Year:  2011        PMID: 21255903     DOI: 10.1016/j.bpc.2010.12.010

Source DB:  PubMed          Journal:  Biophys Chem        ISSN: 0301-4622            Impact factor:   2.352


  5 in total

1.  Exploring the stability limits of actin and its suprastructures.

Authors:  Christopher Rosin; Mirko Erlkamp; Julian von der Ecken; Stefan Raunser; Roland Winter
Journal:  Biophys J       Date:  2014-12-16       Impact factor: 4.033

2.  The role of G-domain orientation and nucleotide state on the Ras isoform-specific membrane interaction.

Authors:  Shobhna Kapoor; Katrin Weise; Mirko Erlkamp; Gemma Triola; Herbert Waldmann; Roland Winter
Journal:  Eur Biophys J       Date:  2012-08-01       Impact factor: 1.733

3.  Hydration-state change of horse heart cytochrome c corresponding to trifluoroacetic-acid-induced unfolding.

Authors:  Yusuke Miyashita; Tetsuichi Wazawa; George Mogami; Satoshi Takahashi; Yoshihiro Sambongi; Makoto Suzuki
Journal:  Biophys J       Date:  2013-01-08       Impact factor: 4.033

4.  A large solvent isotope effect on protein association thermodynamics.

Authors:  Christopher Eginton; Dorothy Beckett
Journal:  Biochemistry       Date:  2013-09-13       Impact factor: 3.162

5.  Small Angle Neutron Scattering Studies of R67 Dihydrofolate Reductase, a Tetrameric Protein with Intrinsically Disordered N-Termini.

Authors:  Purva P Bhojane; Michael R Duff; Khushboo Bafna; Pratul Agarwal; Christopher Stanley; Elizabeth E Howell
Journal:  Biochemistry       Date:  2017-11-07       Impact factor: 3.162

  5 in total

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