• Tryptophan is excited to a long-lived triplet state that is quenched upon contact with cysteine

  • The rates that are measured can determine the probability distribution of Trp-Cys distances and the intramolecular diffusion coefficient

Observing Intramolecular Contact in Unfolded Proteins
Scanning electron microscope image of mixing chip overlaid with confocal image of tryptophan fluorescence

  • Mixing two solvents is a common way to prompt folding

  • Conventional stop-flow mixers mixing times are limited by turbulence to ~ 1 ms

  • Turbulence is eliminated when dimensions are very small (laminar flow regime)

  • Observe folding at various times (positions) after mixing with UV fluorescence

 

Microfabricated Mixer for Observing Folding in as Little as 10 microseconds
     Laboratory of Lisa Lapidus
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