Ultrafast dynamics of protein collapse from single-molecule photon statistics

• DOI: 10.1073/pnas.0611093104
• Publication Date: 2007-02-15T01:37:46Z
• Authors: Daniel Nettels; Irina V. Gopich; Armin Hoffmann; Benjamin Schuler
• Keywords: Nanosecond; Folding (DSP implementation); Energy landscape

We use the statistics of photon emission from single molecules to probe ultrafast dynamics an unfolded protein via Förster resonance energy transfer. Global reconfiguration chain occurs on a time scale ≈50 ns and slows down concomitant with collapse under folding conditions. These diffusive provide missing link between phenomenological chemical kinetics commonly used in physical description terms quantitative free surfaces. The experiments demonstrate potential single-molecule methods accessing biologically important nanosecond scales even heterogeneous populations.