2004
DOI: 10.1002/jccs.200400001
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Thermodynamic Studies on Amino Acid Solvation in some Aqueous Alcohols

Abstract: Present paper discusses the behaviour of transfer free energy of some amino acids from water to aqueous solution of Ethanol, 2-PrOH ad t-BuOH at different compositions. Dissection of transfer free energy into cavity term, interaction term and electrical term reveals that cavity forming free energy of transfer DG t 0 (Cav.) plays an important role in dictating actual interaction of amino acids in these mixed solvents. Cavity forming free energy of transfer has been estimated by using Scaled Particle Theory (SPT… Show more

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Cited by 30 publications
(11 citation statements)
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“…The molal solubilities in the aqueous-electrolyte as well as in pure water were used to determine apparent standard Gibbs energy of solutions (ΔGs0true(itrue)) on molal scale using Eq. (2) [33, 34, 35, 36]. …”
Section: Resultsmentioning
confidence: 99%
“…The molal solubilities in the aqueous-electrolyte as well as in pure water were used to determine apparent standard Gibbs energy of solutions (ΔGs0true(itrue)) on molal scale using Eq. (2) [33, 34, 35, 36]. …”
Section: Resultsmentioning
confidence: 99%
“…Like previous studies, 21,[27][28][29][30][31][32]36,43,44,46 the standard Gibbs energies of solutions (ΔG s 0 ) on molal scale at a particular temperature can be calculated in the present study by using eq 1,…”
Section: Theoretical Sectionmentioning
confidence: 99%
“…In considering these points of views and to explore the solvation mechanisms of various amino acids, the solubility and thermodynamic studies were also carried out by different group of researchers in different aquo-organic and nonaqueous solvent systems. The results in terms of solvation thermodynamics reflected that difference in proticity, dipolar aproticity, acid–base property, hydrophilicity, hydrophobicity, and chemical nature of reference and cosolvents of such binary solvent systems influence the relative stability as well as solvation mechanism of amino acids.…”
Section: Introductionmentioning
confidence: 99%
“…The conformation of a protein in solution is generally a function of electrostatic forces, hydrogen bonding, van der Walls forces, acid-base interactions, and hydrophobic and hydrophilic interactions among the amino acid residues that overall lead to a folded state overcoming an entropic penalty [1][2][3]. Denaturation or defolding of a protein is also an essential process for dissolution and purification of proteins during their extraction from natural sources.…”
Section: Introductionmentioning
confidence: 99%