2011
DOI: 10.1016/j.jct.2010.08.021
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Thermodynamics of the ternary systems: (water + glycine, l-alanine and l-serine + di-ammonium hydrogen citrate) from volumetric, compressibility, and (vapour + liquid) equilibria measurements

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Cited by 80 publications
(39 citation statements)
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References 51 publications
(55 reference statements)
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“…For understanding the solute-solvent and solute-solute interactions in solutions, thermodynamic and physicochemical measurements are very applicable [1][2][3][4][5]. We know that that the stabilization of native conformations of biological macromolecules (proteins) is related to various non-covalent interactions including hydrogen-bonding, electrostatic and hydrophobic interactions [6,7].…”
Section: Introductionmentioning
confidence: 99%
“…For understanding the solute-solvent and solute-solute interactions in solutions, thermodynamic and physicochemical measurements are very applicable [1][2][3][4][5]. We know that that the stabilization of native conformations of biological macromolecules (proteins) is related to various non-covalent interactions including hydrogen-bonding, electrostatic and hydrophobic interactions [6,7].…”
Section: Introductionmentioning
confidence: 99%
“…Besides, our previous study [20] showed that the structure-breaking property of amino acids is so smaller than ordinary salts such as (NH 4 ) 2 HCit.…”
Section: Apparent Molar Volumementioning
confidence: 97%
“…from which values of the infinite dilution apparent molar isobaric expansibility of solute, 0 φ E , were obtained as [20]:…”
Section: Apparent Molar Volumementioning
confidence: 99%
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“…Dependences of solvent activity (a 1 ) on molality of both components for the system di-Ammonium Citrate (2) -Glycine -Water(1) at 298.15 K. Dots: experimental data[26]; surface : correlation with Eq (21)…”
mentioning
confidence: 99%