u‰‰ŽาF“A@ฝŒี Žiƒ\ƒEƒ‹‘ๅŠwj “๚ŽžF‚VŒŽ@‚Q“๚i‹เj@Œ฿Œใ‚SŽž‚R‚O•ช‚ฉ‚็ ๊ŠF ยŽRŠw‰@‘ๅŠw@—HŠw•”i‘Š–อŒดƒLƒƒƒ“ƒpƒXj‚k“‚UŠK@‚k‚U‚O‚RŽบ ‘่–ฺF uDynamic heterogeneity and cooperativity in protein foldingv —vŽ|F Dynamic characterization of the folding process provides invaluable insights into the mechanism of protein folding. We propose the four-point dynamic correlation function that (i) develops a peak at the mean folding time, (ii) probes the dynamic heterogeneity via the peak width, and (iii) characterizes the strength of the cooperativity through the peak height. Here the dynamic heterogeneity refers to the multiplicity of folding pathways or the distribution of free-energy barrier heights, whereas the cooperativity to the extent of correlated residues during the folding process. We present dynamic Monte Carlo simulation results for the four-point dynamic correlation function near the folding temperature, and argue that the dynamic characteristics therefrom rationalize contrasting folding kinetics in downhill and two-state proteins, such as the non-exponential vs. exponential relaxation. ---------------------------------