Time-resolved fluorescence spectroscopy is used to monitor molecular i
nteractions and motions that occur in the picosecond-nanosecond time r
ange, and is especially useful in the analysis of biomolecular structu
re and dynamics. Recent advances in the application of time-resolved f
luorescence spectroscopy to biological systems have led to a better un
derstanding of the origin of nonexponential fluorescence decay in prot
eins, the use of tryptophan analogs as unique spectroscopic probes of
protein-protein interactions, the detailed characterization of protein
-folding processes and intermediates, and the development of new appro
aches to the study of DNA-protein interactions.