Densely packed granular particles that inch past each other under tension interact in ways more complex and surprising than previously believed, two Duke University physicists have discovered.
Their observations, described in the Thursday, February 27, 2003, issue of the research journal Nature, could provide new insight into such geophysical processes as the behavior of a slowly moving glacier or an active earthquake fault, said Robert Behringer, a Duke physics professor who is one of the Nature articles authors. The physicists findings could also have implications for industrial problems, such as how the contents of a hopper holding granular materials such as grain or coal flow, he added.
By using plastic beads made of a material that affects light differently when under stress, Behringer and graduate student Robert Hartley have for the first time shown what happens to grains in a granular network subjected to frictional or "shear" forces that may build slowly.
Monte Basgall | 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.
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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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