2011
DOI: 10.1007/s10953-011-9737-8
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Thermodynamic Studies of Amino Acid–Denaturant Interactions in Aqueous Solutions at 298.15 K

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Cited by 30 publications
(34 citation statements)
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“…The data of ϕ 2 0 are collected in Table , and the variation of ϕ 2 0 as a function of the molality of urea at 298.15 K is shown in Figure along with literature data. , …”
Section: Resultsmentioning
confidence: 99%
“…The data of ϕ 2 0 are collected in Table , and the variation of ϕ 2 0 as a function of the molality of urea at 298.15 K is shown in Figure along with literature data. , …”
Section: Resultsmentioning
confidence: 99%
“…During the last about ten years, we reported the measurements of osmotic coefficients, densities, activity and activity coefficient properties of electrolytes, amino-acids, non-electrolytes as well as of surfactants in aqueous solutions of 18-crown-6 as well as of α-and β-cyclodextrin solutions [18][19][20][21][22][23][24][25]. It has been shown that the conformations of these host molecules, their H-bonding with water molecules in the cavities, as well as hydrophobic interaction along with water structure making effect govern equilibrium properties into solution phase.…”
Section: Introductionmentioning
confidence: 99%
“…The complete equations utilized to determine the molar Gibbs free energy of separation for all scenarios in the analysis are presented in the ESI, † eqn (S5)-(S20). All calculations model recovery at T = 298 K. Non-ideal behavior in solutions was accounted for using activity coefficients, γ i , which were determined using the Davies approximation, 37 nonrandom two-liquid method, 76,77 or experimental data reported in the literature, 78 as described in the ESI. † The G 0 for each species i in aqueous solution can be found in Table S3 in the ESI.…”
Section: Analysis Of Minimum Energy For Nutrient Recoverymentioning
confidence: 99%