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Interaction of some hydrophobic amino acids, peptides, and protein with aqueous 3-chloro-1,2-propanediol and 3-chloro-1-propanol: Biophysical studies

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Title Interaction of some hydrophobic amino acids, peptides, and protein with aqueous 3-chloro-1,2-propanediol and 3-chloro-1-propanol: Biophysical studies
 
Creator KESWANI, N
KISHORE, N
 
Subject PARTIAL MOLAR VOLUMES
EGG-WHITE LYSOZYME
GLOBULE-LIKE STATE
ADIABATIC COMPRESSIBILITIES
BETA-LACTOGLOBULIN
ALPHA-HELIX
THERMODYNAMIC PROPERTIES
HEAT-CAPACITIES
308.15 K
TRIFLUOROETHANOL
Partial molar volume
Partial molar isentropic compressibility
Heat of dilution
alpha-Amino acids
Hydration number
3-Chloropropan-1-ol
3-Chloropropan-1,2-diol
Lysozyme
Isothermal titration calorimetry
 
Description The apparent molar volume V(2,phi), apparent molar isentropic compressibility K(S,2,phi), and heat of dilution (q) of aqueous glycine, alanine, alpha-amino butyric acid, valine, leucine, diglycine, triglycine, and hen egg white lysozyme have been determined in aqueous solutions of 3-chloropropano-1-ol and 3-chloropropan-1,2-diol solutions at T = 298.15 K. These data have been used to calculate the infinite dilution standard partial molar volume V(2,m)(0), partial molar isentropic compressibility K(S,2,m)(0), and enthalpy of dilution Delta(dil)H degrees of the amino acids and peptides in aqueous 3-chloropropano-1-ol and 3-chloropropan-1,2-diol, and the standard partial molar quantities of transfer of the amino acids and peptides to the aqueous alcohol and diol solutions. The linear correlation of V(2,m)(0), for a homologous series of amino acids has been utilized to calculate the contribution of the charged end groups (NH(3)(+), COO(-)), CH(2) group and other alkyl chains of the amino acids to the values of V(2,m)(0). The results on the standard partial molar volumes of transfer, compressibility and enthalpy of dilution from water to aqueous alcohol and diol solutions have been correlated and interpreted in terms of ion-polar, ion-hydrophobic, and hydrophobic-hydrophobic group interactions. The heat of dilution of these amino acids, peptides, and hen egg white lysozyme measured in aqueous solutions of 3-chloropropano-1-ol and 3-chloropropan-1,2-diol by using isothermal titration calorimetry along with the volumetric, compressibility, and calorimetric results on amino acid and peptides have been correlated to understand the nature of interactions operating in these systems. (C) 2010 Elsevier Ltd. All rights reserved.
 
Publisher ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
 
Date 2012-02-08T18:44:10Z
2012-02-08T18:44:10Z
2011
 
Type Article
 
Identifier JOURNAL OF CHEMICAL THERMODYNAMICS,43(4)591-602
0021-9614
http://dx.doi.org/10.1016/j.jct.2010.11.015
http://dspace.library.iitb.ac.in/jspui/handle/100/13840
 
Language English