Fluorescence correlation spectroscopy unfolded proteins

WHAT FLUORESCENCE CORRELATION SPECTROSCOPY CAN TELL US ABOUT UNFOLDED PROTEINS... [Pg.114]

Fluorescence correlation spectroscopy (FCS) measures rates of diffusion, chemical reaction, and other dynamic processes of fluorescent molecules. These rates are deduced from measurements of fluorescence fluctuations that arise as molecules with specific fluorescence properties enter or leave an open sample volume by diffusion, by undergoing a chemical reaction, or by other transport or reaction processes. Studies of unfolded proteins benefit from the fact that FCS can provide information about rates of protein conformational change both by a direct readout from conformation-dependent fluorescence changes and by changes in diffusion coefficient. [Pg.114]

The material presented in this chapter demonstrates the utility of fluorescence correlation spectroscopy in the study of unfolded proteins. [Pg.131]

Applications of fluorescence correlation spectroscopy have included studies of sparse molecules on cell surfaces [264, 265], diffusion of Ugand-receptor complexes in cell membranes [266], conformational dynamics of DNA [150, 233], excited-state properties of flavins and flavoproteins [267], photodynamics of green- and red-fluorescent proteins [268,269], protein unfolding pathways [270] and lipid-protein interactions [271]. [Pg.278]

Chattopadhyay, K., Saffarian, S., Elson, E.L., Erieden, C. Measuring unfolding of proteins in the presence of denaturant using fluorescence correlation spectroscopy. Biophys. J. 88, 1413-1422 (2005)... [Pg.295]