Abstract
We have previously investigated the time-resolved intensity and anisotropy decay of dansylated bovine serum albumin (BSA) using multifrequency phase and modulation fluorescence spectroscopy (J. Phys. Chem. 1993, 97, 4231-4238). The present study focuses on how protein denaturation affects the time-resolved fluorescence intensity and anisotropy decays. Specifically, we report results for the denaturation of BSA by urea and guanidine hydrochloride (Gd.HCl). The results demonstrate that the fluorescence intensity decay of dansylated BSA, native and denatured, is best described by a double exponential decay law. The short lifetime component reflects dansyl at the BSA exterior and the long component arises from dansyl located in a more hydrophobic environment
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