The Purdue University research team that recently created a tiny motor out of synthetic biological molecules has found further evidence that RNA molecules can perform physical work, a discovery that could advance nanotechnology and possibly solve fundamental mysteries about life itself.
One promising application of RNA-ATP binding is this microscopic motor, assembled by Peixuan Guos team at Purdue University. The motor, only a few nanometers wide, is formed by six strands of RNA surrounding an "axle" made of DNA. When fed a supply of ATP as fuel, the RNA molecules kick against the DNA in succession, much like the pistons in a conventional motor. (Graphic/Guo Laboratory)
Purdues Peixuan Guo has discovered how viral RNA molecules bind an energy-bearing organic molecule known as ATP. While linking these two substances might seem to create no more than a longer string of letters, the upshot is that now one of lifes most mysterious and ancient storehouses of information can be moved by one of its most important fuels. The discovery could shed light on the fundamental role RNA plays in the creation of living things.
"RNA could be even more of a key player than we realize," said Guo, professor of veterinary pathobiology in Purdues School of Veterinary Medicine. "The fact that it can be made to bind ATP in the phi29 virus could imply that these two molecules were among the first to partner in Earths dance of life."
Chad Boutin | EurekAlert!
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Researchers from the Department of Atomically Resolved Dynamics of the Max Planck Institute for the Structure and Dynamics of Matter (MPSD) at the Center for Free-Electron Laser Science in Hamburg, the University of Hamburg and the European Molecular Biology Laboratory (EMBL) outstation in the city have developed a new method to watch biomolecules at work. This method dramatically simplifies starting enzymatic reactions by mixing a cocktail of small amounts of liquids with protein crystals. Determination of the protein structures at different times after mixing can be assembled into a time-lapse sequence that shows the molecular foundations of biology.
The functions of biomolecules are determined by their motions and structural changes. Yet it is a formidable challenge to understand these dynamic motions.
At the International Symposium on Automotive Lighting 2019 (ISAL) in Darmstadt from September 23 to 25, 2019, the Fraunhofer Institute for Organic Electronics, Electron Beam and Plasma Technology FEP, a provider of research and development services in the field of organic electronics, will present OLED light strips of any length with additional functionalities for the first time at booth no. 37.
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Researchers from the Department of Atomically Resolved Dynamics of the Max Planck Institute for the Structure and Dynamics of Matter (MPSD) at the Center for Free-Electron Laser Science in Hamburg, the University of Potsdam (both in Germany) and the University of Toronto (Canada) have pieced together a detailed time-lapse movie revealing all the major steps during the catalytic cycle of an enzyme. Surprisingly, the communication between the protein units is accomplished via a water-network akin to a string telephone. This communication is aligned with a ‘breathing’ motion, that is the expansion and contraction of the protein.
This time-lapse sequence of structures reveals dynamic motions as a fundamental element in the molecular foundations of biology.
Two research teams have succeeded simultaneously in measuring the long-sought Thorium nuclear transition, which enables extremely precise nuclear clocks. TU Wien (Vienna) is part of both teams.
If you want to build the most accurate clock in the world, you need something that "ticks" very fast and extremely precise. In an atomic clock, electrons are...
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