Characterization of kinetic folding intermediates of recombinant canine milk lysozyme by stopped-flow circular dichroism

An investigation of the kinetic refolding of recombinant canine milk lysozyme is presented by means of circular dichroism (CD) at 10 different wavelengths with a stopped-flow technique, and obtained the CD spectra of the burst-phase and second kinetic intermediates observed during the refolding process. A schematic model of the refolding of canine milk lysozyme that is consistent with the hierarchical mechanism of protein folding is proposed.