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Title: Thermodynamics of the Interaction of a Homologous Series of Amino Acids with Sorbitol
Authors: JHA, NS
Keywords: Partial Molar Volumes
Dilute Aqueous-Solutions
Adiabatic Compressibilities
Protein Stabilization
T=298.15 K
Issue Date: 2010
Citation: JOURNAL OF SOLUTION CHEMISTRY, 39(10), 1454-1473
Abstract: The apparent molar volumes V(2,phi) , apparent molar isentropic compressibilities K (S,2,phi) , and enthalpies of dilution of aqueous glycine, alanine, alpha-amino butyric acid, valine, and leucine have been determined in aqueous 1.0 and 2.0 sorbitol solutions at 298.15 K. These data have been used to calculate the infinite dilution standard partial molar volumes V(2, m)(0), partial molar isentropic compressibilities K(S,2,m)(0), and enthalpies of dilution Delta(dil)H(0) of the amino acids in aqueous sorbitol, along with the standard partial molar quantities of transfer of the amino acids from water to aqueous sorbitol. The linear correlation of V 0 2, m for this homologous series of amino acids has been utilized to calculate the contribution to V 0 2 of the charged end groups (NH(3)(+), COO(-)),, the CH(2) group, and other alkyl chains of the amino acids. The results for the standard partial molar volumes of transfer, compressibilites and enthalpies of dilution from water to aqueous sorbitol solutions have been correlated and interpreted in terms of ion-polar, ion-hydrophobic, and hydrophobic-hydrophobic group interactions. A comparison of these thermodynamic properties of transfer suggest that an enhancement of the hydrophilic/polar group interactions is operating in ternary systems of amino acid, sorbitol, and water.
ISSN: 0095-9782
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