| Abstract
| - We have developed a microfluidic mixer for studyingprotein folding and other reactions with a mixing time of8 μs and sample consumption of femtomoles. This deviceenables us to access conformational changes underconditions far from equilibrium and at previously inaccessible time scales. In this paper, we discuss the designand optimization of the mixer using modeling of convectivediffusion phenomena and a characterization of the mixerperformance using microparticle image velocimetry, dyequenching, and Förster resonance energy-transfer (FRET)measurements of single-stranded DNA. We also demonstrate the feasibility of measuring fast protein foldingkinetics using FRET with acyl-CoA binding protein.
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