アポミオグロビンのフォールディング反応機構

抄録

Study on transient folding intermediates is one of challenging issues in protein folding. In addition to the use of fluorescence and circular dichroism combined with rapid mixing apparatus for kinetic experiments, quench-flow experiments followed by monitoring amide-proton exchange and chemical modification were used for atomic level analyses of apomyoglobin. The topics for this review include 1) possible order of the folding of helices, 2) non-native and native-like structures in the folding intermediate, 3) mutations that stabilized or destabilized intermediates, and 4) mechanism of the switch between intermediate and native structures regulated by H24 and H119 interaction.