Spectroscopic evidence for the preferential hydration of RNase A in glycerol–water mixtures: Dielectric relaxation studies

Betting, H.; Häckel, Marko; Hinz, Hans‐Jürgen; Stockhausen, M.

doi:10.1039/b008827g

Cited by 19 publications

(16 citation statements)

References 7 publications

(4 reference statements)

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“…A number of experimental techniques including e.g. densimetry, 16 osmometry, 17 calorimetry, 18,19 neutron scattering 20,21 and dielectric relaxation 22 have thus been employed for a range of cosolvents in order to determine whether proteins are preferentially solvated by water or by the cosolvent. However, connecting these measurements to a microscopic picture of the solvation layer is not straightforward, and often relies on approximate models.…”

Section: Introductionmentioning

confidence: 99%

Protein Preferential Solvation in Water:Glycerol Mixtures

et al. 2020

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For proteins in solvent mixtures, the relative abundances of each solvent in their solvation shell have a critical impact on their properties. Preferential solvation of a series of proteins in water-glycerol mixtures is studied here over a broad range of solvent compositions via classical molecular dynamics simulations. Our simulation results reveal that the dierences between shell and bulk compositions exhibit dramatic changes with solvent composition, temperature and protein nature. In contrast with the simple and widely used picture where glycerol is completely excluded from the protein interface, we show that for aqueous solutions with less than 50% glycerol in volume, protein solvation shells have approximately the same composition as the bulk solvent and proteins are in direct contact with glycerol. We further demonstrate that at high glycerol concentration, glycerol depletion from the solvation shell is due to an entropic factor arising from the reduced accessibility of bulky glycerol molecules in protein cavities. The resulting molecular picture is important to understand protein activity and cryopreservation in mixed aqueous solvents.

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Section: Introductionmentioning

confidence: 99%

Protein Preferential Solvation in Water:Glycerol Mixtures

et al. 2020

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“…Therefore, it has been widely used to study the dynamics and structure of multicomponent mixed solution. For example, Betting et al studied the dielectric behavior of RNA in glycerol aqueous solutions. By comparing the DS before and after adding RNA, they found that RNA preferentially adsorbed water molecules in the bulk.…”

Section: Introductionmentioning

confidence: 99%

Cononsolvency of poly(N‐isopropylacrylamide) in methanol aqueous solution—insight by dielectric spectroscopy

Yang

Zhao

2017

J Polym Sci B Polym Phys

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Both water and methanol are good solvents for poly(N‐isopropylacrylamide) (PNIPAM), while PNIPAM does not dissolve in their mixed solvents, this phenomenon is called cononsolvency. Cononsolvency is closely related to many phenomena in life but so far, its mechanism is still controversial. In this work, the dielectric behavior of PNIPAM methanol aqueous solution was studied in the frequency of 40Hz–40GHz. From lower frequency to higher frequency, four relaxations were found. They are, respectively, from global chain motion, local motion of backbone, motion of side chain group, and the dipole orientation of the solvent molecule. The solvent dependence of dielectric parameters for the chain motion implied that the PNIPAM chain has undergone the coil‐globule‐coil transition. Dielectric analysis to microwave frequency showed that the volume of the bound solvent units on PNIPAM chain increases with the increasing methanol concentration, which suggested that the structure of solvation units bound on PNIPAM side chains undergo a changing process experience from water to water‐methanol cluster to the ternary methanol cluster. This work reveals the structure and dynamics of the PNIPAM chain and the solvent unit that involved in the solvation of PNIPAM, and provides some new insight into the cononsolvency phenomenon. © 2017 Wiley Periodicals, Inc. J. Polym. Sci., Part B: Polym. Phys. 2017, 55, 1227–1234

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“…[21] Glycerol, sorbitol and other polyolic co-solvents have been shown to lead to a "preferential hydration" of the protein, that is, to the exclusion of the co-solvent molecules from the protein surface. [3][4][5][25][26][27][28][29] Being strongly hydrophilic co-solvents, they interact strongly with water molecules and have a relatively weak affinity for the polar residues on the protein surface, thus leading to the preferential hydration of the protein.…”

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confidence: 99%

Pressure Perturbation Calorimetry: A New Technique Provides Surprising Results on the Effects of Co‐solvents on Protein Solvation and Unfolding Behaviour

Ravindra

Winter

2004

ChemPhysChem

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We used pressure perturbation calorimetry (PPC), a relatively new and efficient technique, to study the solvation and volumetric properties of proteins in their native and unfolded states. In PPC, the coefficient of thermal expansion of the partial volume of the protein is deduced from the heat consumed or produced after small isothermal pressure jumps (e.g., AE 5 bar), and it strongly depends on the interaction of the protein with the solvent or co-solvent at the protein-solvent interface. Furthermore, the effects of various chaotropic and kosmotropic co-solvents (glycerol, sorbitol, sucrose, urea, guanidinium hydrochloride, guanidinium sulfate, potassium sulfate) on the volume and expansivity changes were measured over a wide concentration range with high precision. Depending on the type of co-solvent and its molar concentration, specific differences were found for the solvation properties and unfolding behaviour of the proteins, and the volume change upon unfolding may even change sign. The aim of the PPC study described herein was two-fold: to obtain more insight into the basic thermodynamic properties of protein solvation and the volume effects accompanying unfolding scenarios of proteins in various co-solvents-as these form the basis for understanding their physiological functions and their use in drug design and formulation-and, more generally, to initiate further valuable applications in studies of other biomolecular and chemical systems.The stability and folding of proteins has fascinated protein chemists for many years, and gaining an understanding of this still remains one of the most challenging goals in the field. In general, a protein's stability depends on the temperature and pressure, its hydration capacity and on the solvent's properties. [1][2][3][4][5][6][7][8][9] An important factor contributing to their stability is also their relative affinity towards a particular reagent (in the present context, a co-solvent) in comparison to water or a buffer solution. In fact, protein studies are conducted almost exclusively in rather complex aqueous solutions. It is also wellknown that the cytoplasm of a cell is relatively crowded, and surface-to-surface gaps of neighbouring organelles and biopolymers are, on average, less than 5 nm. [10,11] Given such proximity, we can expect the structure and dynamics of the solvent to be largely determined by the properties of the biomolecular surfaces, and-vice versa-the surface properties of the bio-

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Spectroscopic evidence for the preferential hydration of RNase A in glycerol–water mixtures: Dielectric relaxation studies

Cited by 19 publications

References 7 publications

Protein Preferential Solvation in Water:Glycerol Mixtures

Protein Preferential Solvation in Water:Glycerol Mixtures

Cononsolvency of poly(N‐isopropylacrylamide) in methanol aqueous solution—insight by dielectric spectroscopy

Pressure Perturbation Calorimetry: A New Technique Provides Surprising Results on the Effects of Co‐solvents on Protein Solvation and Unfolding Behaviour

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