Protein conformation and reversed-phase high-performance liquid chromatography.

ABSTRACT

The structure of a series of proteins has been investigated by circular dichroism, fluorescence and visible spectroscopy as well as by differential scanning calorimetry under reversed-phase high-performance liquid chromatography elution conditions. These studies show that 1-propanol, a typical eluent, induces a reversible conformational change in proteins to an apparently ordered, helical form. This structural transition occurs in the range of propanol concentrations that produces elution of a particular protein. The possible relationship between this conformational change and protein elution is considered.