Abstract
The structural dynamics of proteins on the nanosecond time scale can be probed with dipolar relaxation in response to photoexcitation of intrinsic tryptophan (Trp) residues. For membrane proteins, however, the complexity due to overlapping contributions from the protein itself, the membrane mimic, and the aqueous solvent impairs detailed analysis and interpretation. To disentangle these contributions, we measured time-resolved emission spectra of Trp in the protein Mistic in detergent micelles of various polarities. By comparison with Trp analogues in water and micelles, we could dissect the contributions from hydration, micelle, and protein matrix to dipolar relaxation on the nanosecond time scale. Our results demonstrate that ultrafast, subnanosecond relaxation reports on the extent of Trp shielding from water, with micelle and protein moieties making additive contributions. By contrast, relaxation in the low nanosecond regime is due to dipolar rearrangement of micelle and protein moieties upon photoexcitation, thereby probing conformational dynamics around the intrinsic fluorophore.
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