Probing solute–solute and solute–solvent interactions in (l-arginine+d-xylose/l-arabinose+water) solutions at different temperatures by using volumetric and viscometric methods

Solute–solute and solute–solvent interactions of l-histidine and l-arginine in aqueous-streptomycin sulphate solutions at different temperatures: A physicochemical study

“…At higher temperatures the solvent from the secondary solvation layer of amino acid (L-histidine and L-arginine) zwitterions is released into the bulk of the solvent, resulting in the expansion of the solution, as inferred from larger V ϕ°v alues at higher temperatures [38][39][40]. Similar trends in V ϕ°v alues were obtained in our earlier studies on interactions of L-histidine in aqueous-glucose/ sucrose [12,16] solutions and L-arginine in aqueous-xylose/arabinose [2] solutions.…”

“…(2). The values of V ϕ°a nd S v along with the standard deviations of linear regression, σ for L-histidine/L-arginine in water and in aqueous-streptomycin sulphate solutions at different temperatures are given in Table 5.…”

“…The values V ϕ°f or L-histidine and L-arginine in water at different temperatures have been taken from our previous studies [2,16]. The temperature dependence of V ϕ°c an be represented by the relation…”

“…Thermodynamic and physicochemical measurements are useful in understanding the solute-solvent and solute-solute interactions in solutions [1][2][3][4][5]. When certain solutes are added to protein solutions they cause stabilization and destabilization to the proteins.…”

Volumetric, ultrasonic and UV absorption studies on interactions of antibiotic drug chloramphenicol with glycine and its dipeptide in aqueous solutions at T = (288.15–318.15) K

“…For understanding the solute-solvent and solute-solute interactions in solutions, thermodynamic and physicochemical measurements are very applicable [1][2][3][4][5]. We know that that the stabilization of native conformations of biological macromolecules (proteins) is related to various non-covalent interactions including hydrogen-bonding, electrostatic and hydrophobic interactions [6,7].…”