Infrared spectroscopic studies of solvent-induced conformational changes in globular proteins.

Infrared absorption spectroscopy has been used to study the effect of organic solvents on the conformation of myoglobin, apomyoglobin, hemoglobin, lysozyme and ribonuclease. Beta structure can easily be induced by specific solvent effects. Films prepared from a 50% (v/v) mixture of alcohol, acetone, pyridine, tetrahydrofuran or dimethylsulfoxide/water mixtures show a high proportion of beta structure. The degree of induction of beta structure depends on the hydrocarbon content of the alcohol in the order methanol greater than ethanol greater than butanol. No beta structure was observed in films prepared from aqueous octanol solutions. Lyophilization tends to decrease secondary structure. The conformation of the proteins depends on the particular solvent system and the solvent composition. Solution studies of myoglobin in pure dimethylsulfoxide show that the conformation is a mixture of random and beta forms while in dimethylsulfoxide/2H2O mixtures the conformation is a mixture of alpha-helical and beta forms.