2010
DOI: 10.1016/j.jct.2009.08.013
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Volumetric and viscometric studies of urea in binary aqueous solutions of glucose at different temperatures

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Cited by 13 publications
(6 citation statements)
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“…The tendency of higher Dl # 2 values over the Dl # 1 values indicates that the stronger solute-solvent interaction is present within the glucose in aqueous binary urea solution. Whereas in our earlier study [10], the smaller Dl # 2 values over the Dl # 1 values established very weak solute-solvent interaction. Therefore, the situation is suggesting that the formation of the transition state is less favoured in the presence of glucose; rather the formation of transition state is accompanied by the rapture and distortion of the intermolecular bonds in solvent structure.…”
Section: Resultscontrasting
confidence: 69%
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“…The tendency of higher Dl # 2 values over the Dl # 1 values indicates that the stronger solute-solvent interaction is present within the glucose in aqueous binary urea solution. Whereas in our earlier study [10], the smaller Dl # 2 values over the Dl # 1 values established very weak solute-solvent interaction. Therefore, the situation is suggesting that the formation of the transition state is less favoured in the presence of glucose; rather the formation of transition state is accompanied by the rapture and distortion of the intermolecular bonds in solvent structure.…”
Section: Resultscontrasting
confidence: 69%
“…Thus the negative value of the difference of these two volumes ðU v À V m Þ, thereby shows the presence of strong solute-solvent interactions. While, in our earlier work [10] negative U v values were obtained possibly due to the weak solute-solvent or solute-solute interactions. Further the U v values decrease with increasing temperature almost in every mass% of urea solutions that may be attributed to the breaking of hydrogen bonding and subsequent destruction of the ice-like structure of the solvent water.…”
Section: Resultsmentioning
confidence: 55%
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“…For instance, urea and its alkyl-substituted compounds are often considered as the breaker of water structure [6], the denaturants of native proteins [7] and have a good solubilizing effect on hydrocarbons and polar molecules [8,9]. In recent decades, many researchers have discussed the interactions of urea and its derivatives in aqueous solution conditions through thermodynamic and other properties [10][11][12][13][14][15][16][17]6], as well as by theoretical computation [18,19]. However, the mechanism of protein denaturation by urea and its homologues is still obscure and remains as an open problem [20][21][22][23], i.e.…”
Section: Introductionmentioning
confidence: 99%