Abstract
Time-resolved fluorescence intensity and anisotropy decays of dansylated bovine serum albumin (BSA) are investigated by multifrequency phase and modulation fluorescence spectroscopy. We found that a double exponential decay law best describes the fluorescence intensity decay of covalently attached dansyl to BSA. The short lifetime component is attributed to dansyl located at the exterior surface of BSA. The longer-lived component reflects dansyl at the interior of BSA. This result indicates that there are two dansyl-BSA populations in the ground state. An associated model is then found to best describe the anisotropy decay kinetics of dansylated BSA. This result is consistent with the observed ground-state heterogeneity
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