The Future Is Finally Here: The Hoverboard.

Built and flown by Catalin Alexandru Duru, the board is controlled by only the movement of the pilots feet and is believed to be a viable transport method in the not too distant future. 

New plans for prototypes are underway, flying up to 1.5 meters above the ground with definite hopes of eventually creating a market to sell these hoverboards.

Catalin Alexandru Duru has achieved the farthest hoverboard flight ever, with a total of 275.9 m.


Studying dynamics of ion channels

Despite a large body of work, the exact molecular details underlying ion selectivity and transport of the potassium channel remain unclear. “Since conventional methods, such as X-ray crystallography, capture only averaged frozen structures, it is not possible to investigate how the dynamic of the protein could be involved in key aspects of their function”, explains physicist Alipasha Vaziri, a joint group leader at the Max F. Perutz Laboratories (MFPL) and the Institute of Molecular Pathology (IMP) and head of the research platform “Quantum Phenomena & Nanoscale Biological Systems” (QuNaBioS) of the University of Vienna.

Vaziri’s team, together with researchers at the Institute for Biophysical Dynamics (University of Chicago), have now used infrared (IR) spectroscopy coupled with molecular dynamic-based simulations of the obtained spectra to investigate the subtlest changes in the shape of the KcsA potassium channel that are induced by binding either potassium or the only 0.04 nanometers smaller sodium ion. This combination proved to be a powerful tool to disentangle convoluted IR spectra - which contain contributions from the whole protein - by assigning each part of the spectrum to the amino acids that contribute to it.

Publication in the Journal of Physical Chemistry B: Paul Stevenson, Christoph Götz, Carlos R. Baiz, Jasper Akerboom, Andrei Tokmakoff and Alipasha Vaziri: Visualizing KcsA Conformational Changes upon Ion Binding by Infrared Spectroscopy and Atomistic Modeling. In: The Journal of Physical Chemistry B (April 2015). DOI: http://dx.doi.org/10.1021/acs.jpcb.5b02223

Caption: 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. Credit: Copyright: David S. Goodsell & RCSB Protein Data Bank