Apparent molar volumes and apparent molar isentropic compressions of the protein stabilizer, trimethylamine-N-oxide (TMAO) were determined from the densities and speed of sound measured at T = (288.15, 298.15 and 308.15) K in aqueous solutions of N-methylacetamide (NMA) at four different concentrations (2, 4, 6 and 8 mol/kg). The concentration dependencies of the calculated quantities extrapolated to the infinite dilution lead to the standard partial molar properties. The latter values were combined with the previously published data for TMAO in pure water, to obtain the partial molar properties of transfer from water to aqueous NMA solutions. From the transfer data the interaction parameters were determined according to the McMillan-Mayer theory formalism. The calculated parameters and their temperature characteristics are discussed in terms of solute-solvent, solute-solute and solute-cosolute interactions and compared with analogous data for protein denaturant, n-butylurea.
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 Agnieszka Boruń,
- dr hab. inż. Joanna Krakowiak link open in new tab
Additional information
- DOI
- Digital Object Identifier link open in new tab 10.1016/j.tca.2020.178535
- Category
- Publikacja w czasopiśmie
- Type
- artykuły w czasopismach
- Language
- angielski
- Publication year
- 2020
