Fox Chase Cancer Center researchers and their colleagues in Japan and San Francisco have obtained new insight into the molecular structure of prion particles responsible for mad cow disease and other degenerative neurological disorders. In new research to be published in this weeks Online Early Edition of the Proceedings of the National Academy of Sciences (www.pnas.org), Fox Chase biophysicist Heinrich Roder, Ph.D., and colleagues describe a computer model of the structural core of prions, based on biophysical measurements of a fibrous form of a prion protein fragment. Prions are infectious protein particles linked to degenerative neurological diseases in animals and humans, such as mad cow disease (bovine spongiform encephalopathy or BSE) in cattle, scrapie in sheep and goats, and Creutzfeldt-Jakob disease (CJD) in humans.
For proteins, form really does equal function. Not only are they essential building blocks of the body, but proteins are also the workers of every cell, carrying out its specific functions. This function depends on the ultimate three-dimensional shape of the protein, a form achieved by folding flexible chains of amino acids until each is properly aligned so that the protein can do its job. Normally, the folding of proteins is highly efficient and specific, but sometimes the process goes awry, resulting in dangerous misfolded forms.
Prion diseases result from the conversion of a normal cellular protein into an alternative structure that forms threadlike fibers called amyloid fibrils. They accumulate in target tissues, such as brain tissue, where they cause the progressive degeneration of cognitive and motor functions and ultimately prove fatal.
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MPQ scientists achieve long storage times for photonic quantum bits which break the lower bound for direct teleportation in a global quantum network.
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Tiny pores at a cell's entryway act as miniature bouncers, letting in some electrically charged atoms--ions--but blocking others. Operating as exquisitely sensitive filters, these "ion channels" play a critical role in biological functions such as muscle contraction and the firing of brain cells.
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The miniaturization of the current technology of storage media is hindered by fundamental limits of quantum mechanics. A new approach consists in using so-called spin-crossover molecules as the smallest possible storage unit. Similar to normal hard drives, these special molecules can save information via their magnetic state. A research team from Kiel University has now managed to successfully place a new class of spin-crossover molecules onto a surface and to improve the molecule’s storage capacity. The storage density of conventional hard drives could therefore theoretically be increased by more than one hundred fold. The study has been published in the scientific journal Nano Letters.
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With innovative experiments, researchers at the Helmholtz-Zentrums Geesthacht and the Technical University Hamburg unravel why tiny metallic structures are extremely strong
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