Rodolfo I Z Hermans

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Using the recently developed single molecule force-clamp technique we quantitatively measure the kinetics of conformational changes of polyprotein molecules at a constant force. In response to an applied force of 110 pN, we measure the dwell times of 1647 unfolding events of individual ubiquitin modules within each protein chain. We then establish a(More)
We explore and exploit diffraction effects that have been previously neglected when modelling optical measurement techniques for the bending of micro-mechanical transducers such as cantilevers for atomic force microscopy. The illumination of a cantilever edge causes an asymmetric diffraction pattern at the photo-detector affecting the calibration of the(More)
The mechanical stretching of single polyproteins is an emerging tool for the study of protein (un)folding, chemical catalysis and polymer physics at the single molecule level. The observed processes, i.e., unfolding or reduction events, are typically considered to be stochastic and by nature are susceptible to be censored by the finite duration of the(More)
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