Fujita Y, Izumiguchi S, Noda Y
Int J Pept Protein Res. 1982 Jan;19(1):25-31. doi: 10.1111/j.1399-3011.1982.tb03019.x.
The thermal denaturation of lysozyme in aqueous sulfoxide solutions (pH 3) was investigated by differential scanning calorimetry (DSC). The sulfoxides employed were dimethylsulfoxide (DMSO), ethylmethylsulfoxide, (DMSO), dimethylsulfoxide (DMSO), and butylmethylsulfoxide (BMSO). The temperature of denaturation, Td, decreased with an increase in the concentration of sulfoxide, the decrease becoming much more pronounced at higher sulfoxide concentrations. The lowering of Td was enhanced by an increase in the hydrocarbon content of the sulfoxide molecule. The enthalpy of denaturation, delta Hd, showed a complex dependence on the solvent composition; the delta Hd first increased with increasing sulfoxide concentration and then started decreasing at different concentrations for each sulfoxide. This behavior is analogous to that with monohydric alcohols, but is different from that with guanidine hydrochloride. These results may be interpreted in terms of the interactions of the sulfoxide added with the protein and with water.
