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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

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Title 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
 
Creator KISHORE, N
MARATHE, R
 
Subject partially folded state
egg-white lysozyme
alpha-lactalbumin
thermodynamic properties
beta-lactoglobulin
peptide
trifluoroethanol
propensity
alcohols
3-chloropropan-1-ol
3-chloropropan-1,2-diol
protein stability
apparent molar volume
surface tension of aqueous chloro alcohols
 
Description 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) cm(3) . mol(-1); (partial derivative V/(o)(2,m)/partial derivative T)(p) = (10.31 +/- 1.28) . 10(-2) cm(3) . K-1 . mol(-1); (partial derivative(2)V(2,m)(o)/partial derivative T-2)(p) = (4.16 +/- 1.46) . 10(-3) cm(3) . K-2 . mol(-1), and for 3-chloroproan 1,2-diol(aq): V-2,m(o) = (80.62 +/- 0.23) cm(3) . mol(-1); (partial derivative V-2,m(o)/partial derivative T)p = (8.499 +/- 1.080) 10(-2) cm(3) . K-1 . mol(-1); (partial derivative(2)V(2,m)(o)/partial derivative T-2)(p) = (1.610 +/- 0.67) . 10(-3) cm(3) . 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 then egg-white lysozyme and alpha-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-chlorupropan-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. (C) 2000
 
Publisher ACADEMIC PRESS LTD
 
Date 2011-07-12T20:31:06Z
2011-12-26T13:02:50Z
2011-12-27T05:49:58Z
2011-07-12T20:31:06Z
2011-12-26T13:02:50Z
2011-12-27T05:49:58Z
2000
 
Type Article
 
Identifier JOURNAL OF CHEMICAL THERMODYNAMICS, 32(3), 413-424
0021-9614
http://dx.doi.org/10.1006/jcht.2000.0624
http://dspace.library.iitb.ac.in/xmlui/handle/10054/3564
http://hdl.handle.net/10054/3564
 
Language en