TY  - JOUR
A1  - Hoffmann, Armin S.
A1  - Kane, Avinash S.
A1  - Nettels, Daniel
A1  - Hertzog, David E.
A1  - Baumgärtel, Peter
A1  - Lengefeld, Jan
A1  - Reichardt, Gerd
A1  - Horsley, David A.
A1  - Seckler, Robert
A1  - Bakajin, Olgica
A1  - Schuler, Benjamin
T1  - Mapping protein collapse with single molecule fluorescence and kinetic synchrotron radiation circular dichroism spectroscopy
Y1  - 2007
UR  - http://www.mendeley.com/research/mapping-protein-collapse-with-singlemolecule-fluorescence-and-kinetic- synchrotron-radiation-circular-dichroism-spectroscopy/#
SN  - 0027-8424
ER  - 
TY  - JOUR
A1  - Kane, Avinash S.
A1  - Hoffmann, Armin S.
A1  - Baumgärtel, Peter
A1  - Seckler, Robert
A1  - Reichardt, Gerd
A1  - Horsley, David A.
A1  - Schuler, Benjamin
A1  - Bakajin, Olgica
T1  - Microfluidic mixers for the investigation of rapid protein folding kinetics using synchrotron radiation circular dichroism spectroscopy
N2  - 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.
Y1  - 2008
UR  - http://pubs.acs.org/doi/abs/10.1021/ac801764r
SN  - 0003-2700
ER  - 
TY  - JOUR
A1  - Lipman, Everett A.
A1  - Schuler, Benjamin
A1  - Bakajin, Olgica
A1  - Eaton, William A.
T1  - Single-molecule measurement of protein folding kinetics
N2  - 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.
Y1  - 2003
UR  - http://www.sciencemag.org/content/301/5637/1233
SN  - 0036-8075
ER  -