N. Kishore, R. Marathe
Mar 1, 2000
Citations
0
Influential Citations
7
Citations
Journal
The Journal of Chemical Thermodynamics
Abstract
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): V2, mo = (79.79 ± 0.23)cm3· mol − 1; (∂V2, mo / ∂T)p = (10.31 ± 1.28) · 10 − 2cm3· K − 1· mol − 1; (∂2V2, mo / ∂T2)p = (4.16 ± 1.46) · 10 − 3cm3· K − 2· mol − 1, and for 3-chloroproan-1,2-diol(aq): V2, mo = (80.62 ± 0.23)cm3· mol − 1; (∂V2, mo / ∂T)p = (8.499 ± 1.080) · 10 − 2cm3· K − 1· mol − 1; (∂2V2, mo / ∂T2)p = (1.610 ± 0.67) · 10 − 3cm3· 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.