New publication in J. Phys. Chem. B

New Publication, News
Together with our colleagues at the Institute for Biophysical Dynamics at the University of Chicago, we have developed a method using infrared spectroscopy and atomistic modeling that would allow to better understand the mechanism behind the extreme ion selectivity and transport properties in ion channels. Our findings have recently been published in The Journal of Physical Chemistry B. [caption id="attachment_1312" align="aligncenter" width="584"] Location of the potassium channel KcsA in the cell membrane of bacteria. The schematic illustration on the right shows the changes in strength and direction of vibrational coupling inside the filter depending on the ion species, as found by the study. @David S. Goodsell & RCSB Protein Data Bank[/caption] Ion channels are essential structures of life. Ion channels are specialized pores in the cell membrane and move charged…
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New Publication in Analytical Chemistry

New Publication, News
Together with our collaborator Markus Arndt we published in Analytical Chemistry on how to improve Laser-induced acoustic desorption (LIAD) for natural biochromophores. This methodology might enable us to use fragile biomolecules in Quantum-enhanced metrology experiments. Link to Paper or look up other publications of our group. Ugur Sezer, Lisa Wörner, Johannes Horak, Lukas Felix, Jens Tüxen, Christoph Götz, Alipasha Vaziri, Marcel Mayor, and Markus Arndt Laser-induced acoustic desorption of natural and functionalized biochromophores Anal. Chem., 2015, 87 (11), pp 5614–5619 (Download)
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New Paper in eLife on a Non-Conventional Translocation Mechanism for Motor Proteins

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Motors proteins of the conserved kinesin-14 family have important roles in mitotic spindle organization and chromosome segregation. Previous studies have indicated that kinesin-14 motors are non-processive enzymes, working in the context of multi-motor ensembles that collectively organize microtubule networks. Here we show that the yeast kinesin-14 Kar3 generates processive movement as a heterodimer with the non-motor proteins Cik1 or Vik1. By analyzing the single-molecule properties of engineered motors we demonstrate that the non-catalytic domain has a key role in the motility mechanism by acting as a 'foothold' that allows Kar3 to bias translocation towards the minus end. This mechanism rivals the speed and run length of conventional motors, can support transport of the Ndc80 complex in vitro and is critical for Kar3 function in vivo. Our findings provide an example for…
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New Paper in Biomedical Optics Express

New Publication, News
Our recent paper "Optimizing and extending light-sculpting microscopy for fast functional imaging in neuroscience" on the improvement of our previously published imaging technique can be accessed via this Website. [caption id="attachment_1218" align="alignright" width="1020"] Experimental setup and various modalities of light sculpting microscopy.[/caption]  
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