2009
DOI: 10.1007/s10973-008-9232-7
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Preferential solvation of lysozyme by dimethyl sulfoxide in binary solutions of water and dimethyl sulfoxide

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Cited by 25 publications
(33 citation statements)
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“…Compared to glycerol, little is known about the DMSO-lysozyme interactions, apart from a preferential hydration of lysozyme in water-DMSO mixtures indicating a weak or no binding of DMSO to lysozyme. 3,4 This suggests that DMSO mainly influences the dielectric properties of the solution, and is consistent with the observed weaker temperature dependence of the cut-off length δ(T) in the case of DMSO.…”
Section: A Refractive Indices and Static Dielectric Constantssupporting
confidence: 84%
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“…Compared to glycerol, little is known about the DMSO-lysozyme interactions, apart from a preferential hydration of lysozyme in water-DMSO mixtures indicating a weak or no binding of DMSO to lysozyme. 3,4 This suggests that DMSO mainly influences the dielectric properties of the solution, and is consistent with the observed weaker temperature dependence of the cut-off length δ(T) in the case of DMSO.…”
Section: A Refractive Indices and Static Dielectric Constantssupporting
confidence: 84%
“…26 Furthermore, Arakawa et al 3 and Kamiyama et al 4 observed a preferential hydration of lysozyme in water-DMSO mixtures, indicating that DMSO does not bind to the lysozyme surface. 4 This suggests that DMSO mainly affects the dielectric properties of the bulk solution. Nevertheless, DMSO leads to denaturation at volume fractions beyond 70 vol.%.…”
Section: Introductionmentioning
confidence: 99%
“…10,12,13 As expected, the methyl groups face hydrophobic surfaces leaving the sulfoxide available for hydrogen bonding. We used a variety of spectroscopic and calorimetric techniques to test the hypothesis that cosolvents directly interact with amino-acid residues important in network formation and subsequently decrease solution viscosity.…”
Section: Polar Solvents Preferentially Solvate and Directly Interact supporting
confidence: 66%
“…Indeed, polar solvents have been shown to preferentially solvate hydrophobic surfaces and interact with protein residues through hydrogen bonding and dispersive-type interactions. [10][11][12][13] Large-length-scale water density fluctuations near hydrophobic surfaces have been shown to control hydrophobic assembly in aqueous solution. 14 If protein self-association is at least partially mediated via dispersive-type interactions, then at high concentrations as the two surfaces (protein-protein) approach each other, formation of the soft liquid-vapor-like interface characteristic of the hydrophobic force of assembly could be induced.…”
Section: Introductionmentioning
confidence: 99%
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