Publications by authors named "Anabel E-M Clemen"

Bundles of filamentous actin are dominant cytoskeletal structures, which play a crucial role in various cellular processes. As yet quantifying the fundamental interaction between two individual actin filaments forming the smallest possible bundle has not been realized. Applying holographic optical tweezers integrated with a microfluidic platform, we were able to measure the forces between two actin filaments during bundle formation.

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Since its first production from muscle tissue more than 65 years ago, our knowledge about actin has come a long way. While at the beginning it was identified as a muscle protein, nowadays actin is considered as one of the most important components of the cytoskeleton, playing a crucial role in cell motility, adhesion, morphology and intracellular transport processes. In vitro models have been constructed for about 20 years to gain better insight into the chemophysical and biomechanical properties of actin networks by being able to reduce and tune its complexity.

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Holographic optical tweezers (HOT) are a versatile technology, with which complex arrays and movements of optical traps can be realized to manipulate multiple microparticles in parallel and to measure the forces affecting them in the piconewton range. We report on the combination of HOT with a fluorescence microscope and a stop-flow, multi-channel microfluidic device. The integration of a high-speed camera into the setup allows for the calibration of all the traps simultaneously both using Boltzmann statistics or the power spectrum density of the particle diffusion within the optical traps.

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Myosin-V is a linear molecular motor that hydrolyzes ATP to move processively toward the plus end of actin filaments. Motion of this motor under low forces has been studied recently in various single-molecule assays. In this paper we show that myosin-V reacts to high forces as a mechanical ratchet.

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Myosin-V is a processive two-headed actin-based motor protein involved in many intracellular transport processes. A key question for understanding myosin-V function and the communication between its two heads is its behavior under load. Since in vivo myosin-V colocalizes with other much stronger motors like kinesins, its behavior under superstall forces is especially relevant.

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We present a novel approach for the generation of higly frequency-stable, widely tunable, single-frequency cw UV light that is suitable for high-resolution spectroscopy. Sum-frequency generation (SFG) of two solid-state sources with a single cavity resonant for both fundamental waves is employed. Using a highly stable, narrow-linewidth frequency-doubled cw Nd:YAG laser as a master laser and slaving to it the SFG cavity and the other fundamental wave from a Ti:sapphire laser, we generate UV radiation of 33-mW output power around 313 nm.

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