Abstract
It is well known that time-resolved fluorescence of tryptophan in proteins frequently displays a non-exponential decay, even though the proteins contain only one tryptophan. It is also known that the tryptophan residue possesses a motional freedom in the proteins, as revealed by a time-resolved fluorescence anisotropy. In order to elucidate the mechanism underlying the non-exponential behavior on the intensity decay, we have solved a modified Smoluchowski equation into which an anguler-dependent quenching rate was introduced, and obtained theoretical expressions for both the time-resolved intensity and anisotropy. In the present paper we have described the results of the analysis on the motional-modes of internal motion of tryptophane in Streptomyces subtilisin inhibitor, on the basis of their picosecond time-resolved flouorescence intensity and anisotropy.
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