What fluorescence correlation spectroscopy can tell us about unfolded proteins.

摘要: Publisher Summary Fluorescence correlation spectroscopy (FCS) measures rates of diffusion, chemical reaction, and other dynamic processes fluorescent molecules. Studies unfolded proteins benefit from the fact that FCS can provide information about protein conformational change both by a direct readout conformation-dependent fluorescence changes in diffusion coefficient. Although coefficient is relatively insensitive to conformation changes, it be measured with high accuracy so useful for monitoring structural occur as passes among partially states. As takes on more compact or extended conformations, hydrodynamic radius consequently correspondingly; if these are large enough, they observed measurements. Among kinetics approaches used study dynamics within state, closely related relaxation methods which small free energy perturbations displace equilibrium point reaction system. The kinetic parameters deduced rate new equilibrium.