Towards a Quantitative Understanding of Protein Hydration and Volumetric Properties

Mitra, Lally; Rouget, Jean-Baptiste; García-Moreno, Bertrand; Royer, Catherine A.; Winter, Roland

doi:10.1002/cphc.200800405

Cited by 58 publications

(86 citation statements)

References 23 publications

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“…This temperature dependence can be rationalized by the larger thermal expansivity of the unfolded state relative to that of the native state. A comparatively stronger volume expansion with temperature of the unfolded state has been experimentally demonstrated by densimetric measurements on WT SNase [5,35,36]. These results indicate that the partial molar volume increase of the native protein is larger at low temperature and decreases significantly as temperature rises.…”

Section: Temperature Dependence Of the Volume Change Of Unfoldingmentioning

confidence: 76%

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

Suladze

Kahse

Erwin

et al. 2015

Methods

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Section: Temperature Dependence Of the Volume Change Of Unfoldingmentioning

confidence: 76%

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

Suladze

Kahse

Erwin

et al. 2015

Methods

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“…[81][82][83][92][93][94][95] By contrast, changes in volume associated with pressure-induced denaturation of globular proteins at elevated pressures are always negative. [85][86][87][88][96][97][98][99][100][101][102][103][104] This observation reflects the fact that, according to Le Chatelier's principle, a protein may be denatured by pressure only if the partial volume of its pressure-induced denatured state is smaller than that of the native state at and above the denaturation pressure. Therefore, the volume change, DV, associated with pressure-induced protein denaturation is invariably negative.…”

Section: Conformational Transitionsmentioning

confidence: 76%

CHAPTER 21. Partial Molar Volumes of Proteins in Solution

Chalikian¹

2014

Volume Properties

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An understanding of the molecular origins and driving forces of protein recognition events, including reactions of folding and binding, relies increasingly on the combination of structural, computational, and thermodynamic studies. 1-8 Without exemption, these reactions can be viewed as an exchange of solute-solvent for solute-solute interactions with concomitant changes in thermodynamic properties. 9-14 Solute-solvent interactions exert a mutually modifying effect on the protein and its waters of hydration. The latter are structurally, kinetically, and thermodynamically distinct from waters in the bulk. 15-17 Thermodynamic distinctions involve, among others, the differential packing density of water molecules solvating protein groups and water in the bulk. In this connection, volumetric (densimetric) measurements have proven useful for thermodynamic characterization of protein hydration as well as changes in hydration accompanying recognition events involving proteins.Among thermodynamic variables of state, volume is the most easily comprehensible and intuitively appealing. The partial molar volume, V1, of a protein reflects the entire range of its intra-and intermolecular (solutesolvent) interactions and the packing of the polypeptide chain inside the Volume Properties: Liquids, Solutions and Vapours Edited by Emmerich Wilhelm and Trevor M. Letcher

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“…17 In this case, however, the absolute values of the α U (T) function for unfolded proteins are much higher than α N (T), consistent with the experimental observation of the positive values for the changes in expansivity upon unfolding. 10,16 Interestingly, such leveling off for the α(T) function was observed for the α(T) of various polar amino acid side chains. 11,15 All of this suggests that hydration plays a significant role in this nonlinear behavior.…”

Section: ■ Results and Discussionmentioning

confidence: 92%

Molecular Determinants of Expansivity of Native Globular Proteins: A Pressure Perturbation Calorimetry Study

Vasilchuk¹,

Pandharipande²,

Suladze³

et al. 2014

J. Phys. Chem. B

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There is a growing interest in understanding how hydrostatic pressure (P) impacts the thermodynamic stability (ΔG) of globular proteins. The pressure dependence of stability is defined by the change in volume upon denaturation, ΔV = (∂ΔG/∂P)T. The temperature dependence of change in volume upon denaturation itself is defined by the changes in thermal expansivity (ΔE), ΔE = (∂ΔV/∂T)P. The pressure perturbation calorimetry (PPC) allows direct experimental measurement of the thermal expansion coefficient, α = E/V, of a protein in the native, αN(T), and unfolded, αU(T), states as a function of temperature. We have shown previously that αU(T) is a nonlinear function of temperature but can be predicted well from the amino acid sequence using α(T) values for individual amino acids (J. Phys. Chem. B 2010, 114, 16166-16170). In this work, we report PPC results on a diverse set of nine proteins and discuss molecular factors that can potentially influence the thermal expansion coefficient, αN(T), and the thermal expansivity, EN(T), of proteins in the native state. Direct experimental measurements by PPC show that αN(T) and EN(T) functions vary significantly for different proteins. Using comparative analysis and site-directed mutagenesis, we have eliminated the role of various structural or thermodynamic properties of these proteins such as the number of amino acid residues, secondary structure content, packing density, electrostriction, dynamics, or thermostability. We have also shown that αN(T) and EN,sp(T) functions for a given protein are rather insensitive to the small changes in the amino acid sequence, suggesting that αN(T) and EN(T) functions might be defined by a topology of a given protein fold. This conclusion is supported by the similarity of αN(T) and EN(T) functions for six resurrected ancestral thioredoxins that vary in sequence but have very similar tertiary structure.

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Towards a Quantitative Understanding of Protein Hydration and Volumetric Properties

Cited by 58 publications

References 23 publications

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

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

CHAPTER 21. Partial Molar Volumes of Proteins in Solution

Molecular Determinants of Expansivity of Native Globular Proteins: A Pressure Perturbation Calorimetry Study

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