First, we have studied protein unfolding, which has traditionally been studied with spectroscopic techniques (circular dichroism, NMR, fluorescence). Although viscosity has been listed in textbooks for many years as a suitable technique, few –if any– quantitative rheological studies of unfolding have been reported, mainly due to technical difficulties. With microrheology, we have been able to quantify the size of folded and unfolded proteins, as well as the Gibbs free energy of unfolding.
Secondly, we have developed new technology for studying the microstructural dynamics of solvent-responsive complex fluids. With macroscopic rheometry it is virtually impossible to change the solvent composition in a sample and monitor its rheological response. By integrating microfluidics and microrheology, we have been able to overcome this barrier: the microscopic lengthscales in microfluidic devices shorten the diffusive timescales in a dialysis set-up enough to achieve rapid and reversible changes in sample composition. Our dialysis cell for microrheology is a unique tool for studying the dynamics of structural and rheological changes induced by solvent composition.
Thirdly, we have
employed microrheology to monitor the progress of photopolymerization
reactions with high spatial and temporal resolution. We have been able
to show that the polymerization reation is highly localized and
quantitatively deterine these apatial variations.