Abstract
To measure the distance distribution of Bull Serum Albumin (BSA)-Norfloxacin pairs in solution, an improved numerical model in analyzing time-domain Fluorescence Resonance Energy Transfer (FRET) was developed. Compared to the classical model, the distance distribution function in the improved model is not necessary to be assumed. In the experiment, BSA-Norfloxacin pairs' distance distribution were investigated within the temperature ranging from 20~50 oC and BSA concentration ranging from 10-5 to 5*10-5 mol/L. Experimental results analyzing by the improved model indicate: the typical distance of BSA-Norfloxacin pairs was at the range of 10-9~10-8 mol/L; the peak location of distance distribution function was 8.60nm and half width was 12.40nm at 20 oC, 1.0*10-5 mol/L; the peak location and the half width of the distance distribution function could change regularly with the change of the temperature and the concentration.
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