ABSTRACT

The densities of aqueous and aqueous electrolyte solutions of tris(hydroxymethyl)ami¬nomethane (TRIS), N-[tris(hydroxymethyl)methyl]-3-aminopropanesulfonic acid (TAPS), N-[tris(hydroxymethyl)methyl]-3-amino-2-hydroxypropanesulfonic acid (TAPSO), and N-tris[hydroxymethyl]-4-amino-butanesulfonic acid (TABS), have been measured by a high-precision vibrating-tube digital densitometer from (298.15 to 328.15) K under atmospheric pressure. This study was undertaken to investigate the interactions between these compounds and electrolytes of potassium acetate (KAc), potassium bromide (KBr), potassium chloride (KCl), and sodium chloride (NaCl). The experimental densities were correlated as a function of the concentration of the buffers and ionic salts. The solubilities of buffers at 298.15 K in aqueous and in aqueous electrolyte solutions have also been determined from the experimental results of density measurements. The solubility data served to estimate the apparent transfer free energies ( ) and transfer molar volumes ( ) of buffers from water to aqueous electrolyte solutions at 298.15 K. The contributions of various functional groups of these compounds were estimated from the and results.
On the basis of density measurements, apparent molar volumes ( ) of 4-morpholineethanesulfonic acid (MES), 4-morpholinepropanesulfonic acid (MOPS), 3-morpholino-2-hydroxypropanesulfonic acid (MOPSO), and 4-(N-morpholino)butane sulfonic acid (MOBS) in water and in aqueous solutions of KAc, KCl, KBr, and NaCl have been determined at 298.15 K. The transfer molar volumes ( ) from water to aqueous electrolyte solutions, obtained from the apparent molar volume at infinite dilution ( ), have been calculated. In addition, the contributions of some functional groups of these buffers were estimated form the and results.
The densities of aqueous 1,4-dioxane and ethanol solutions of TRIS, TAPS, TASO, TABS, MES, MOPS, MOPS, and MOBS were measured at different temperatures. The solubilities of these buffers in water and at several concentrations of 1,4-dioxane and ethanol at 298.15 K have also been determined from the experimental results of density measurements. At saturation conditions, we have found that MOPS, MOBS, and TABS induced two-liquid-phase separation for 1,4-dioxane + water mixed solvent system. Liquid–liquid equilibrium (LLE) data are presented for the ternary mixtures of water + 1,4-dioxane + MOPS and water + 1,4-dioxane + MOBS at 298.15 K under atmospheric pressure. The solubility data were further used to calculate the contribution of transfer free energies ( ) of various functional groups from water to the aqueous 1,4-dioxane and ethanol solutions at 298.15 K.
On the basis of apparent transfer free energies ( ), through the solubility measurements, the interactions of zwitterionic glycine peptides: glycine (Gly), diglycine (Gly2), triglycine (Gly3), and tetraglycine (Gly4) with several common neutral pH, amine-based buffers have been studied. The transfer free energies ( ) of the peptide backbone unit (–CH2C=O–NH–) contributions have been estimated from values. We have also measured the interaction of TRIS buffer with Bovine Serum Albumin (BSA), as a globular protein, using dynamic light scattering (DLS).

ABSTRACT

The densities of aqueous and aqueous electrolyte solutions of tris(hydroxymethyl)ami¬nomethane (TRIS), N-[tris(hydroxymethyl)methyl]-3-aminopropanesulfonic acid (TAPS), N-[tris(hydroxymethyl)methyl]-3-amino-2-hydroxypropanesulfonic acid (TAPSO), and N-tris[hydroxymethyl]-4-amino-butanesulfonic acid (TABS), have been measured by a high-precision vibrating-tube digital densitometer from (298.15 to 328.15) K under atmospheric pressure. This study was undertaken to investigate the interactions between these compounds and electrolytes of potassium acetate (KAc), potassium bromide (KBr), potassium chloride (KCl), and sodium chloride (NaCl). The experimental densities were correlated as a function of the concentration of the buffers and ionic salts. The solubilities of buffers at 298.15 K in aqueous and in aqueous electrolyte solutions have also been determined from the experimental results of density measurements. The solubility data served to estimate the apparent transfer free energies ( ) and transfer molar volumes ( ) of buffers from water to aqueous electrolyte solutions at 298.15 K. The contributions of various functional groups of these compounds were estimated from the and results.
On the basis of density measurements, apparent molar volumes ( ) of 4-morpholineethanesulfonic acid (MES), 4-morpholinepropanesulfonic acid (MOPS), 3-morpholino-2-hydroxypropanesulfonic acid (MOPSO), and 4-(N-morpholino)butane sulfonic acid (MOBS) in water and in aqueous solutions of KAc, KCl, KBr, and NaCl have been determined at 298.15 K. The transfer molar volumes ( ) from water to aqueous electrolyte solutions, obtained from the apparent molar volume at infinite dilution ( ), have been calculated. In addition, the contributions of some functional groups of these buffers were estimated form the and results.
The densities of aqueous 1,4-dioxane and ethanol solutions of TRIS, TAPS, TASO, TABS, MES, MOPS, MOPS, and MOBS were measured at different temperatures. The solubilities of these buffers in water and at several concentrations of 1,4-dioxane and ethanol at 298.15 K have also been determined from the experimental results of density measurements. At saturation conditions, we have found that MOPS, MOBS, and TABS induced two-liquid-phase separation for 1,4-dioxane + water mixed solvent system. Liquid–liquid equilibrium (LLE) data are presented for the ternary mixtures of water + 1,4-dioxane + MOPS and water + 1,4-dioxane + MOBS at 298.15 K under atmospheric pressure. The solubility data were further used to calculate the contribution of transfer free energies ( ) of various functional groups from water to the aqueous 1,4-dioxane and ethanol solutions at 298.15 K.
On the basis of apparent transfer free energies ( ), through the solubility measurements, the interactions of zwitterionic glycine peptides: glycine (Gly), diglycine (Gly2), triglycine (Gly3), and tetraglycine (Gly4) with several common neutral pH, amine-based buffers have been studied. The transfer free energies ( ) of the peptide backbone unit (–CH2C=O–NH–) contributions have been estimated from values. We have also measured the interaction of TRIS buffer with Bovine Serum Albumin (BSA), as a globular protein, using dynamic light scattering (DLS).

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