Investigations on solute–solvent interactions of amino acids in aqueous solutions of sodium dihydrogen phosphate at different temperatures

Densities and Speeds of Sound of Solutions of Glycine, l-Alanine, and l-Valine in Aqueous Ammonium Dihydrogen Phosphate at Different Temperatures

“…Ample research − has been carried out on thermodynamic properties of amino acids in aqueous electrolyte solutions, carbohydrates, surfactants, etc. but the phosphates salts are still found in limited study. − The phosphates are biologically and industrially important salts which are employed in food, cosmetics, and pharmaceutical industries and also in numerous biochemical studies. − The present work is just a continuation of our earlier laboratory work on the volumetric and ultrasonic properties of amino acids and peptides with phosphate salts of biological importance. − To explore more on phosphate salts, we hereby delineate the densities and speeds of sound of glycine, l -alanine and l -valine in aqueous ammonium dihydrogen phosphate (ADP) solutions at different temperatures (288.15, 298.15, 308.15, and 318.15) K and atmospheric pressure.…”

A Comprehensive Study on Molecular Interactions of l-Ascorbic Acid/Nicotinic Acid in Aqueous [BMIm]Br at Varying Temperatures and Compositions: Spectroscopic and Thermodynamic Insights

“…The uncertainties in the apparent molar isentropic compression, δ K ϕ ,s , have been premeditated by means of the following expression Table comprises the empirically achieved speed of sound data along with computed apparent molar isentropic compression data at distinct temperatures. The negative values of K ϕ ,s indicate that the water molecules encompassing vitamins in the hydration spheres are less compressible than those of the bulk solution.…”

Volumetric interactions of a series of α-amino acids in aqueous magnesium chloride solutions at 278.15, 288.15, 298.15, and 308.15 K

“…The study was established within the characterization of the hydration properties of both hydrophobic and charged groups of biocompounds, providing insights into the role of solute-solvent interactions associated with fundamental protein phenomena such as folding-unfolding transitions, solubility, and denaturation. Moreover, it is well known that the presence of salts largely influence the stability of proteins, that might have serious implications in many diseases, turning this kind of study very up-to-date [3,4] and of high relevance from a biological, pharmaceutical, and medical point of views [5].…”