Abstract

Fluorescence has become established over the past two decades as one of the techniques of choice for studying structure and dynamics in macromolecules and functional fluids. The former include important biological molecules like proteins and peptides and the latter encompass important molecular assemblies such as membranes and micelles. Few of these possess any intrinsic fluorescence which is readily observable. Tryptophan, which occurs naturally in proteins, provides one of the few notable exceptions. Hence the measurement protocol has always been to either label the molecule of interest covalently with a fluorophore or confine a fluorophore in the region of interest using physical constraints eg solubility difference, as in aqueous dispersions of surfactants.

© 1998 IEEE