Volumetric properties and surface tension of aqueous 3-chloropropan-1-ol and aqueous 3-chloropropan-1,2-diol, and correlation of their effect on protein stability

Author： Kishore N. Marathe R.

Publisher： Academic Press

ISSN： 0021-9614

Source： Journal of Chemical Thermodynamics, Vol.32, Iss.3, 2000-03, pp. : 413-424

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Abstract

Densities, apparent molar volumes, and surface tension of aqueous 3-chloropropan-1-ol and 3-chloropropan-1,2-diol were determined at temperatures from (283.08 to 308.15) K. The results of the volumetric measurements have been used to calculate the following thermodynamic quantities at T = 298.15 K. For 3-chloropropan-1-ol(aq): V_{2, m}^o = (79.79 ± 0.23)cm³· mol^{- 1}; (∂V_{2, m}^o / ∂T)_p = (10.31 ± 1.28) · 10^{- 2}cm³· K^{- 1}· mol^{- 1}; (∂²V_{2, m}^o / ∂T²)_p = (4.16 ± 1.46) · 10^{- 3}cm³· K^{- 2}· mol^{- 1}, and for 3-chloroproan-1,2-diol(aq): V_{2, m}^o = (80.62 ± 0.23)cm³· mol^{- 1}; (∂V_{2, m}^o / ∂T)p = (8.499 ± 1.080) · 10^{- 2}cm³· K^{- 1}· mol^{- 1}; (∂²V_{2, m}^o / ∂T²)_p = (1.610 ± 0.67) · 10^{- 3}cm³· K^{- 2}· mol^{- 1}. The preferential interaction parameters of the interaction of 3-chloropropan-1-ol and 3-chloropropan-1,2-diol with two structurally homologous proteins (hen egg-white lysozyme and α -lactalbumin) have been calculated by correlating the measured surface tension data to the surface areas of these proteins. The data on the measured apparent molar volumes and surface tension of aqueous 3-chloropropan-1-ol and 3-chloropropan-1,2-diol, in combination with the thermal denaturation data and surface area values of hen egg-white lysozyme from literature, clearly indicate a parallel trend in changes in the surface tension of water, partial molar volume, and ability to alter the thermal stability of these proteins.