Publications Repository - Gdańsk University of Technology

This work confirms our earlier supposition, that volumetric and acoustic parameters for simple model proposed by us are directly related to stabilizing/destabilizing effect of osmolytes on proteins structure. The apparent molar volumes, V and the apparent molar isentropic compressions, KS,, of glycine and N,N,N –trimethylglycine (betaine) were determined from densities and speed of sound measurements in aqueous solution of N-methylacetamide (as a model of peptide bond of protein). The standard molar parameters for osmolytes were obtained from concentration dependence of the calculated quantities at NMA concentration equal 2, 4, 6 and 8 (mol/kg) and at temperature T = (288.15, 298.15 and 308.15) K. The standard values were combined with volumetric and compressibility data for amino acids in pure water to obtain transfer properties from water to aqueous N-methylacetamide solutions. The standard partial molar volume of transfer of studied osmolytes, 〖Δ_t V〗_Φ^0, seems to be related mainly to hydrophilic/hydrophobic features of molecules. The stabilizing/destabilizing effect of solute on protein structure is reflected in temperature influence on the limiting partial molar quantities.

Authors

• Emilia Kaczkowska link open in new tab ,
• dr hab. inż. Jarosław Wawer link open in new tab ,
• dr Magdalena Tyczyńska,
• profesor Małgorzata Jóźwiak,
• dr hab. inż. Joanna Krakowiak link open in new tab