DSpace at IIT Bombay >
IITB Publications >
Please use this identifier to cite or link to this item:
|Title: ||Interaction of some hydrophobic amino acids, peptides, and protein with aqueous 3-chloro-1,2-propanediol and 3-chloro-1-propanol: Biophysical studies|
|Authors: ||KESWANI, N|
|Keywords: ||PARTIAL MOLAR VOLUMES|
|Issue Date: ||2011|
|Publisher: ||ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD|
|Citation: ||JOURNAL OF CHEMICAL THERMODYNAMICS,43(4)591-602|
|Abstract: ||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.|
|Appears in Collections:||Article|
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.