@article{LipmanSchulerBakajinetal.2003,
  author    = {Lipman, Everett A. and Schuler, Benjamin and Bakajin, Olgica and Eaton, William A.},
  title     = {Single-molecule measurement of protein folding kinetics},
  issn      = {0036-8075},
  year      = {2003},
  abstract  = {In order to investigate the behavior of single molecules under conditions far from equilibrium, we have coupled a microfabricated laminar-flow mixer to a confocal optical system. This combination enables time-resolved measurement of Foerster resonance energy transfer after an abrupt change in solution conditions. Observations of a small protein show the evolution of the intramolecular distance distribution as folding progresses. This technique can expose subpopulations, such as unfolded protein under conditions favoring the native structure, that would be obscured in equilibrium experiments.},
  language  = {en}
}
@article{KaneHoffmannBaumgaerteletal.2008,
  author    = {Kane, Avinash S. and Hoffmann, Armin S. and Baumg{\"a}rtel, Peter and Seckler, Robert and Reichardt, Gerd and Horsley, David A. and Schuler, Benjamin and Bakajin, Olgica},
  title     = {Microfluidic mixers for the investigation of rapid protein folding kinetics using synchrotron radiation circular dichroism spectroscopy},
  issn      = {0003-2700},
  year      = {2008},
  abstract  = {We have developed a microfluidic mixer optimized for rapid measurements of protein folding kinetics using synchrotron radiation circular dichroism (SRCD) spectroscopy. The combination of fabrication in fused silica and synchrotron radiation allows measurements at wavelengths below 220 nm, the typical limit of commercial instrumentation. At these wavelengths, the discrimination between the different types of protein secondary structure increases sharply. The device was optimized for rapid mixing at moderate sample consumption by employing a serpentine channel design, resulting in a dead time of less than 200 ;s. Here, we discuss the design and fabrication of the mixer and quantify the mixing efficiency using wide-field and confocal epi-fluorescence microscopy. We demonstrate the performance of the device in SRCD measurements of the folding kinetics of cytochrome c, a small, fast-folding protein. Our results show that the combination of SRCD with microfluidic mixing opens new possibilities for investigating rapid conformational changes in biological macromolecules that have previously been inaccessible.},
  language  = {en}
}
@article{HoffmannKaneNettelsetal.2007,
  author    = {Hoffmann, Armin S. and Kane, Avinash S. and Nettels, Daniel and Hertzog, David E. and Baumg{\"a}rtel, Peter and Lengefeld, Jan and Reichardt, Gerd and Horsley, David A. and Seckler, Robert and Bakajin, Olgica and Schuler, Benjamin},
  title     = {Mapping protein collapse with single molecule fluorescence and kinetic synchrotron radiation circular dichroism spectroscopy},
  issn      = {0027-8424},
  year      = {2007},
  language  = {en}
}