Applications of pressure perturbation calorimetry in biophysical studies

Zhai, Ya; Okoro, Linus N.; Cooper, Alan; Winter, Roland

doi:10.1016/j.bpc.2010.12.010

Cited by 41 publications

(49 citation statements)

References 66 publications

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“…In this technique, the apparent thermal expansion coefficient of a protein is calculated from the heat changes induced by small periodic changes in pressure above a protein solution. The technique and its application in biological systems are described elsewhere (Schweiker and Makhatadze 2009;Zhai et al 2011). …”

Section: Expansibilitymentioning

confidence: 99%

Volume and Compressibility of Proteins

Gekko

2015

Subcellular Biochemistry

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The partial specific (or molar) volume, expansibility, and compressibility of a protein are fundamental thermodynamic quantities for characterizing its structure in solution. We review the definitions, measurements, and implications of these volumetric quantities in relation to protein structural biology. The partial specific volumes under constant molality (isomolal) and chemical potential (isopotential) conditions of the cosolvent (multicomponent systems) are explained in terms of preferential solvent interactions relevant to the solubility and stability of proteins. The partial expansibility is briefly discussed in terms of the effects of temperature on protein-solvent interactions (hydration) and internal packing defects (cavities). We discuss the compressibility-structure-function relationships of proteins based on analyses of the correlations between the partial adiabatic compressibilities and the structures or functions of various globular proteins (including mutants), focusing on the roles of the internal cavities in structural fluctuations. The volume and compressibility changes associated with various conformational transitions are also discussed in terms of the changes in hydration and cavities in order to elucidate the nonnative structures and the transition mechanisms, especially those associated with pressure denaturation.

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Section: Expansibilitymentioning

confidence: 99%

Volume and Compressibility of Proteins

Gekko

2015

Subcellular Biochemistry

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“…Moreover, a, is strongly affected by the interaction of the biomolecule with the surrounding solvent. Thus, PPC can provide useful information about hydrational properties of the solute [5,6].…”

Section: Principle Of Ppc Measurementsmentioning

confidence: 99%

“…This calorimeter has basically the same architecture as a power-compensation differential scanning calorimeter (DSC), but measures the heat flow into or out of a sample upon small isothermal pressure changes (of typically ±5 bar). The method can be applied to study the coefficient of thermal expansion, a, and relative volume changes, DV/V, of aqueous solutions and dispersions of chemical and biochemical systems, including amino acids, proteins, DNA and phospholipid vesicles, micellar systems, and polymers [1][2][3][4][5][6][7][8][9][10][11].…”

Section: Introductionmentioning

confidence: 99%

Probing volumetric properties of biomolecular systems by pressure perturbation calorimetry (PPC) – The effects of hydration, cosolvents and crowding

Suladze

Kahse

Erwin

et al. 2015

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“…Thus, the authors of [111] have observed a concomitant crystallization of non-solvated 1,4-diazabicyclo[2.2.2]octane hydroiodide (a two-component crystal) and the diazonium diaiodide co-crystal with methanol (a three-component crystal) from the same batch under the same conditions. Understanding the mechanisms of the pressure-induced solvation -desolvation processes is relevant for the solid drug forms research [104-107, 109, 110, 112], as well as for the studies of the conformational transitions and denaturation of proteins in solution at ambient and increased pressures [113]. A special field is research of the solvation/desolvation of MOFs at high pressure [114][115][116][117][118][119], since it is directly related to the functioning of these materials in real catalytic reactions.…”

Section: Some Prospectsmentioning

confidence: 99%

Multicomponent organic crystals at high pressure

Boldyreva

2014

Zeitschrift Für Kristallographie Crystalline Materials

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High-pressure research of the crystals of organic and coordination compounds is now a well-established field. However, the studies of multicomponent crystals (hydrates, solvates, salts and co-crystals) are just emerging. The aim of this paper is to give a personal view of what makes the multicomponent organic systems peculiar for high-pressure research as compared with the monocomponent ones. Several different types of structure response to compression and reverse decompression are reviewed with examples based on research of salts, co-crystals and hydrates of amino acids. Challenges and prospects of further studies are discussed.

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Applications of pressure perturbation calorimetry in biophysical studies

Cited by 41 publications

References 66 publications

Volume and Compressibility of Proteins

Volume and Compressibility of Proteins

Probing volumetric properties of biomolecular systems by pressure perturbation calorimetry (PPC) – The effects of hydration, cosolvents and crowding

Multicomponent organic crystals at high pressure

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