Pressure perturbation calorimetry, heat capacity and the role of water in protein stability and interactions

Cooper, A., Cameron, D., Jakus, J. and Pettigrew, G. W. (2007) Pressure perturbation calorimetry, heat capacity and the role of water in protein stability and interactions. Biochemical Society Transactions, 35(6), pp. 1547-1550. (doi:10.1042/BST0351547)

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Abstract

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.

Item Type:Articles
Keywords:ADAMANTANE ADAMANTANECARBOXYLATE INCLUSION COMPLEXES AQUEOUS-SOLUTION AQUEOUS-SOLUTIONS BINDING biomolecular interaction CYCLODEXTRIN heat capacity hydration hydrogen bonding LIGAND LIGAND-BINDING PRESSURE pressure perturbation calorimetry (PPC) PROTEIN protein folding stability PROTEINS SOLVATION SOLVENT STABILITY THERMODYNAMICS VOLUMETRIC PROPERTIES WATER WEAK
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Cooper, Professor Alan
Authors: Cooper, A., Cameron, D., Jakus, J., and Pettigrew, G. W.
College/School:College of Science and Engineering > School of Chemistry
Journal Name:Biochemical Society Transactions
ISSN:0300-5127

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