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)
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)
The elastic restoring force of tissues must be able to operate over the very wide range of loading rates experienced by living organisms. It is surprising that even the fastest events involving animal muscle tissues do not surpass a few hundred hertz. We propose that this limit is set in part by the elastic dynamics of tethered proteins extending and(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)
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