The folding and dynamics of globular proteins is a multidimensional problem. The structures of the heterogeneous population of refolding protein molecules are characterized by multiple distances and time constants. Deciphering the mechanism of folding depends on studies of the processes rather than the folded structures alone. Spectroscopy is indispensable for these sorts of studies. Herein, it is shown that the determination of intramolecular distance by ensemble and single-molecule FRET experiments enable the exploration of partially folded states of refolding protein molecules.
- FRET (fluorescence resonance energy transfer)
- Protein folding
- Single-molecule studies
- Timeresolved spectroscopy