It is widely acknowledged, and usually self-evident, that solvent water plays a crucial role in the overall thermodynamics of protein stabilization and biomolecular interactions. Yet we lack experimental techniques that can probe unambiguously the nature of protein–water or ligand–water interactions and how they might change during protein folding or ligand binding. PPC (pressure perturbation calorimetry) is a relatively new technique based on detection of the heat effects arising from application of relatively small pressure perturbations (±5 atm; 1 atm=101.325 kPa) to dilute aqueous solutions of proteins or other biomolecules. We show here how this can be related to changes in solvation/hydration during protein–protein and protein–ligand interactions. Measurements of ‘anomalous’ heat capacity effects in a wide variety of biomolecular interactions can also be related to solvation effects as part of a quite fundamental principle that is emerging, showing how the apparently unusual thermodynamics of interactions in water can be rationalized as an inevitable consequence of processes involving the co-operative interaction of multiple weak interactions. This leads to a generic picture of the thermodynamics of protein folding stabilization in which hydrogen-bonding plays a much more prominent role than has been hitherto supposed.
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December 2007
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Conference Article|
November 23 2007
Pressure perturbation calorimetry, heat capacity and the role of water in protein stability and interactions
A. Cooper;
A. Cooper
1
*WestChem Department of Chemistry, University of Glasgow, Glasgow G12 8QQ, Scotland, U.K.
1To whom correspondence should be addressed (email alanc@chem.gla.ac.uk).
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D. Cameron;
D. Cameron
*WestChem Department of Chemistry, University of Glasgow, Glasgow G12 8QQ, Scotland, U.K.
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J. Jakus;
J. Jakus
*WestChem Department of Chemistry, University of Glasgow, Glasgow G12 8QQ, Scotland, U.K.
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G.W. Pettigrew
G.W. Pettigrew
†Royal (Dick) School of Veterinary Studies, University of Edinburgh, Summerhall, Edinburgh EH9 1QH, U.K.
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Publisher: Portland Press Ltd
Received:
August 08 2007
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2007 Biochemical Society
2007
Biochem Soc Trans (2007) 35 (6): 1547–1550.
Article history
Received:
August 08 2007
Citation
A. Cooper, D. Cameron, J. Jakus, G.W. Pettigrew; Pressure perturbation calorimetry, heat capacity and the role of water in protein stability and interactions. Biochem Soc Trans 1 December 2007; 35 (6): 1547–1550. doi: https://doi.org/10.1042/BST0351547
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