Measurement of local viscosity of the hydration shell of protein by time-resolved fluorescence anisotropy spectroscopy

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In this study, rotational correlation time Tc of fluorescent dye was measured to evaluate the local viscosity of the hydration region of protein surface.The Tc measured by this method was found to be in linear relation with the solvent viscosity. The CW-laser-based method revealed shorter Tc of Cy3 linked at Cys374 of actin in F-actin than around G-actin, which is consistent with the result by dielectric relaxation data.On the other hand,Tc (<1ns) of small fluorescent dye such as rhodamin 6G in water could not be measured by pulse-laser-based method without picosecond pulse width.We have designed a frequency-region fluorescent anisotropy spectroscopic method to measure Tc of small fluorescent dyes.