Studies in ion solvation in non-aqueous solvents and their aqueous mixtures. Part 17.—Free energies of transfer of alkali-metal chlorides from water to 10–40 %(w/w) dioxan + water mixtures, and of potassium bromide and iodide to the 20 % mixture, at 25°C

1975 ◽  
Vol 71 (0) ◽  
pp. 780 ◽  
Author(s):  
David Feakins ◽  
Brian E. Hickey ◽  
John Phillip Lorimer ◽  
Philip J. Voice
Keyword(s):  
Alkali Metal ◽  
Potassium Bromide ◽  
Ion Solvation ◽  
Aqueous Mixtures ◽  
Free Energies ◽  
Alkali Metal Chlorides ◽  
Metal Chlorides ◽  
Free Energies Of Transfer

Transfer free energies of alkali metal chlorides and of some individual ions in glycerol and water mixtures

1980 ◽  
Vol 58 (1) ◽  
pp. 79-85 ◽  
Author(s):  
Indra N. Basumullick ◽  
Kiron K. Kundu
Keyword(s):  
Alkali Metal ◽  
Aqueous Mixtures ◽  
Free Energies ◽  
Dispersion Interactions ◽  
Native Conformation ◽  
Alkali Metal Chlorides ◽  
Metal Chlorides ◽  
Emf Measurements ◽  
Reference Electrolyte ◽  
Electrolyte Ph

Staqndard free energies of transfer, ΔGt0, of alkali metal chlorides from water to aqueous mixtures of 10, 30, 50, and 70 wt.% glycerol have been determined from emf measurements of the double cell comprising Ag– AgCl and K(Hg) electrodes at 25°C. These values were divided into individual ion contributions by use of tetraphenyl arsonium tetraphenyl boride (Ph4AsBPh4) assumption, the required ΔGt0 values of the reference electrolyte (Ph4AsPh4B), obtained by measuring solubilities of KBPh4, Ph4AsPi, and KPi (Pi = picrate) in the solvents. The solvation behaviour of the involved ions, as dictated by their respective ΔGt0(i) values, in this as well as in systems of other similar co-solvents like ethanol, ethylene glycol, and urea, suggests that it is determined by one or several effects of acid-base, Born-type, and dispersion interactions. Moreover, comparable stability of PH4B–, particularly in aqueous glycerol and urea, suggests that "specific interactions" are possibly responsible for the well_known folding-unfolding phenomenon of native conformation of proteins in presence of co-solvents.

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