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<description>Phys.org internet news portal provides the latest news on science including: Physics, Nanotechnology, Life Sciences, Space Science, Earth Science, Environment, Health and Medicine.</description>

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     <title>Structure of cell signaling molecule suggests general on-off switch</title>
   	 <description>A three-dimensional image of one of the proteins that serves as an on-off switch as it binds to receptors on the surface of a cell suggests there may be a sort of main power switch that could be tripped. These surface receptors are responsible for helping cells discern light, set the heart racing, or detect pain.</description>
     <link>http://phys.org/news285765875.html</link>
	 <category>Biology</category>
	 <pubDate>Sun, 21 Apr 2013 13:00:13 EST</pubDate>
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     <title>Beer's bitter compounds could help brew new medicines</title>
   	 <description>(Phys.org)—Researchers employing a century-old observational technique have determined the precise configuration of humulones, substances derived from hops that give beer its distinctive flavor.</description>
     <link>http://phys.org/news278686996.html</link>
	 <category>Chemistry</category>
	 <pubDate>Tue, 29 Jan 2013 13:03:26 EST</pubDate>
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     <title>Protein production: going viral: Architecture of essential human transcription factor revealed</title>
   	 <description>(Phys.org)—A research team of scientists from EMBL Grenoble and the IGBMC in Strasbourg, France, have, for the first time, described in molecular detail the architecture of the central scaffold of TFIID: the human protein complex essential for transcription from DNA to mRNA. The study, published today in Nature, opens new perspectives in the study of transcription and of the structure and mechanism of other large multi-protein assemblies involved in gene regulation.</description>
     <link>http://phys.org/news276770982.html</link>
	 <category>Biology</category>
	 <pubDate>Mon, 07 Jan 2013 08:49:53 EST</pubDate>
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     <title>Beer's bitter: Researcher determines the absolute configurations of the bitter acids of hops</title>
   	 <description>(Phys.org)—During brewing, beer obtains its bitter flavor from the bitter acids that come from hops. In the journal Angewandte Chemie, scientists now report that they have used X-ray crystallography to determine the absolute configurations of these humulones and isohumulones, as well as several of their derivatives.</description>
     <link>http://phys.org/news275302503.html</link>
	 <category>Chemistry</category>
	 <pubDate>Fri, 21 Dec 2012 08:55:31 EST</pubDate>
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     <title>Supramolecules spin promises for future</title>
   	 <description>(Phys.org)—Microscopic particles that can be made to switch their magnetic state could mean computers of the future will be able to store much more data in much less space. </description>
     <link>http://phys.org/news274602158.html</link>
	 <category>Chemistry</category>
	 <pubDate>Thu, 13 Dec 2012 06:22:49 EST</pubDate>
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     <title>Researchers capture high contrast image of band of DNA fiber</title>
   	 <description>(Phys.org)—A research team in Italy has succeeded in capturing a high contrast image of a band of DNA fiber – the closest anyone has ever come to taking a photograph of a single strand of DNA. The team has outlined the process they used to create the image in their paper published in Nano Letters.</description>
     <link>http://phys.org/news273744639.html</link>
	 <category>Nanotechnology</category>
	 <pubDate>Mon, 03 Dec 2012 08:40:06 EST</pubDate>
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     <title>Researchers stretch C-O bond to record length</title>
   	 <description>(Phys.org)—Researchers at the University of California have succeeded in stretching a carbon monoxide molecule bond to a record length. In their paper published in the journal Nature Chemistry, the team describes how they built on previous work they'd done when building the compound oxatriquinane and noticed unusually long C-O bonds. This time around they swapped out the hydrogen surrounding the oxonium ion with other materials causing the C-O bonds to stretch to a record length of 1.622Å in ethers.</description>
     <link>http://phys.org/news272530348.html</link>
	 <category>Chemistry</category>
	 <pubDate>Mon, 19 Nov 2012 07:10:02 EST</pubDate>
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     <title>Chasing a common cold virus</title>
   	 <description>(Phys.org)—As the cold and flu season makes its annual visit, a team of researchers, using Argonne's Advanced Photon Source, continue to complete a detailed map of the human adenovirus—one of several viruses responsible for the common cold.</description>
     <link>http://phys.org/news270108862.html</link>
	 <category>Chemistry</category>
	 <pubDate>Mon, 22 Oct 2012 08:00:01 EST</pubDate>
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     <title>Iron-sulfur enzymes as candidates for antibiotic development</title>
   	 <description>The iron-sulfur protein IspH plays a central role in the terpene metabolism of several pathogens. The mechanism of the reaction provides an approach for developing new antibiotics, particularly against malaria and tuberculosis. While researching this enzyme, biochemists at the Technische Universitat Munchen discovered a previously unknown reaction: IspH accepts two completely different classes of molecules as partners. This surprising insight, published in Nature Communications, opens up new perspectives in combating infectious diseases.</description>
     <link>http://phys.org/news269001944.html</link>
	 <category>Chemistry</category>
	 <pubDate>Tue, 09 Oct 2012 11:45:52 EST</pubDate>
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     <title>Protein structure unlocks one mystery of multi-drug tolerance</title>
   	 <description>The structures of key bacterial proteins have revealed one of the biochemical secrets that enables bacteria to outwit antibiotics.</description>
     <link>http://phys.org/news267883375.html</link>
	 <category>Chemistry</category>
	 <pubDate>Wed, 26 Sep 2012 13:03:11 EST</pubDate>
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     <title>Making a molecular micromap: Imaging the yeast 26S proteasome at near-atomic resolution</title>
   	 <description>(Phys.org)—Biological systems are characterized by a form of molecular recycling – and proteins do not escape this fate. In particular, unneeded or damaged proteins biochemically marked for destruction undergo controlled degradation by having their peptide bonds broken by proteasomes. Recently, scientists at the Max-Planck Institute of Biochemistry in Germany used cryo-electron microscopy (cryo-EM) single particle analysis and molecular dynamics techniques to map the Saccharomyces cerevisiae 26S proteasome. (Cryo-EM is a form of transmission electron microscopy where the sample is studied at cryogenic temperatures, which unlike X-ray crystallography allows researchers to observe specimens in their native environment without the need for staining or fixing. S. cerevisiae is the yeast species commonly known as baker's or brewer's yeast.) The researchers then used this map to build a near-atomic resolution structural model of the proteasome. The Max Planck team showed that cryo-electron microscopy allowed them to successfully model the 26S core complex where X-ray crystallography studies conducted over the past 20 years have not. </description>
     <link>http://phys.org/news267682061.html</link>
	 <category>Biology</category>
	 <pubDate>Mon, 24 Sep 2012 08:30:01 EST</pubDate>
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     <title>Intrinsically disordered proteins: A conversation with Rohit Pappu</title>
   	 <description>If you open any biology textbook to the section on proteins, you will learn that a protein is made up of a sequence of amino acids, that the sequence determines how the chain of amino acids folds into a compact structure, and that the folded protein's structure determines its function. In other words sequence encodes structure and function derives from structure.</description>
     <link>http://phys.org/news267368532.html</link>
	 <category>Biology</category>
	 <pubDate>Thu, 20 Sep 2012 14:02:33 EST</pubDate>
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     <title>Small is beautiful: Viewing hydrogen atoms with neutron protein crystallography</title>
   	 <description>(Phys.org)—Creating 3D visualizations of hydrogen atoms in proteins is especially challenging, often requiring their locations to be inferred from those of nearby carbon, nitrogen, oxygen or sulfur atoms stored in protein structure databases. These locations are based on atomic positions in databases of previously solved structures, general chemical knowledge, quantum mechanical calculations, or potential hydrogen bonding interactions. While X-ray crystallography can pinpoint hydrogen atom locations at ultrahigh resolution, in practice only a few such positions are experimentally determined. Recently, however, scientists at the University of Toledo, Los Alamos National Laboratory and Oak Ridge National Laboratory used neutron crystallography – a technique that even at lower resolutions can locate individual hydrogen atoms by leveraging scattering properties of the hydrogen isotope deuterium. </description>
     <link>http://phys.org/news267348141.html</link>
	 <category>Physics</category>
	 <pubDate>Thu, 20 Sep 2012 09:10:01 EST</pubDate>
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     <title>Revelation of protein complex function that controls cell proliferation in fruit fly wings provides insights into tumor </title>
   	 <description>A team of researchers in Singapore has determined the structure of a pair of proteins that may play an important role in tumor growth and the progression of cancer. The proteins, Vestigial (Vg) and Scalloped (Sd), normally control wing development in fruit flies, but the team found they show a remarkable structural and functional similarity to the cancer-promoting proteins called YAP and TAZ.</description>
     <link>http://phys.org/news266658464.html</link>
	 <category>Biology</category>
	 <pubDate>Wed, 12 Sep 2012 09:00:12 EST</pubDate>
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     <title>Discarded data may hold the key to a sharper view of molecules</title>
   	 <description>(Phys.org) -- There's nothing like a new pair of eyeglasses to bring fine details into sharp relief. For scientists who study the large molecules of life from proteins to DNA, the equivalent of new lenses have come in the form of an advanced method for analyzing data from X-ray crystallography experiments.</description>
     <link>http://phys.org/news257078826.html</link>
	 <category>Chemistry</category>
	 <pubDate>Thu, 24 May 2012 14:00:10 EST</pubDate>
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     <title>MIT biologist relishes the challenge of picking apart the cell's most complex structure</title>
   	 <description>One of the most important structures in a cell is the nuclear pore complex &amp;#151; a tiny yet complicated channel through which information flows in and out of the cell&amp;#146;s nucleus, directing all other cell activity.</description>
     <link>http://phys.org/news256883870.html</link>
	 <category>Biology</category>
	 <pubDate>Tue, 22 May 2012 05:39:04 EST</pubDate>
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     <title>Scientists learn how to 'out run damage' with imaging technique</title>
   	 <description>Over the decades X-ray crystallography has been fundamental in the development of many scientific fields. The method has revealed the structure and function of many biological molecules, including vitamins, drugs, proteins and nucleic acids such as DNA. However, in order to obtain good data, large single crystals are required. These are often nearly impossible to grow. There also is the problem that X-rays damage delicate biological samples.</description>
     <link>http://phys.org/news249041525.html</link>
	 <category>Physics</category>
	 <pubDate>Tue, 21 Feb 2012 10:14:50 EST</pubDate>
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     <title>Fastest X-ray images of tiny biological crystals</title>
   	 <description>(PhysOrg.com) -- An international research team headed by DESY scientists from the Center for Free-Electron Laser Science (CFEL) in Hamburg, Germany, has recorded the shortest X-ray exposure of a protein crystal ever achieved. The incredible brief exposure time of 0.000 000 000 000 03 seconds (30 femtoseconds) opens up new possibilities for imaging molecular processes with X-rays. This is of particular interest to biologists, but can be employed in many fields, explain lead authors Dr. Anton Barty and Prof. Henry Chapman from the German accelerator centre Deutsches Elektronen-Synchrotron DESY. </description>
     <link>http://phys.org/news244977149.html</link>
	 <category>Physics</category>
	 <pubDate>Thu, 05 Jan 2012 09:12:44 EST</pubDate>
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     <title>New strategy could lead to dose reduction in X-ray imaging</title>
   	 <description>For more than a century, the use of X-rays has been a prime diagnostic tool when it comes to human health. As it turns out, X-rays also are a crucial component for studying and understanding molecules, and a new approach -- just published by researchers at the University of Georgia -- may dramatically improve what researchers can learn using the technique.</description>
     <link>http://phys.org/news241178212.html</link>
	 <category>Physics</category>
	 <pubDate>Tue, 22 Nov 2011 10:30:01 EST</pubDate>
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     <title>Hitting moving RNA drug targets</title>
   	 <description>By accounting for the floppy, fickle nature of RNA, researchers at the University of Michigan and the University of California, Irvine have developed a new way to search for drugs that target this important molecule. Their work appears in the June 26 issue of Nature Chemical Biology.</description>
     <link>http://phys.org/news228324745.html</link>
	 <category>Chemistry</category>
	 <pubDate>Sun, 26 Jun 2011 16:32:43 EST</pubDate>
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     <title>Boosting research into new drugs: 'Smart materials' make proteins form crystals</title>
   	 <description>Scientists have developed a new method to make proteins form crystals using 'smart materials' that remember the shape and characteristics of the molecule. The technique, reported today in Proceedings of the National Academy of Sciences, should assist research into new medicines by helping scientists work out the structure of drug targets.</description>
     <link>http://phys.org/news227792882.html</link>
	 <category>Chemistry</category>
	 <pubDate>Mon, 20 Jun 2011 15:00:21 EST</pubDate>
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     <title>Lasers used to form 3-D crystals made of nanoparticles (w/ video)</title>
   	 <description>(PhysOrg.com) -- University of Michigan physicists used the electric fields generated by intersecting laser beams to trap and manipulate thousands of microscopic plastic spheres, thereby creating 3-D arrays of optically induced crystals.</description>
     <link>http://phys.org/news226136384.html</link>
	 <category>Physics</category>
	 <pubDate>Wed, 01 Jun 2011 08:40:27 EST</pubDate>
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     <title>Nature's elegant solution to repairing DNA in cancer, other conditions</title>
   	 <description>A major discovery about an enzyme's structure has opened a window on understanding DNA repair. Scientists at Duke University Medical Center have determined the structure of a nuclease that will help scientists to understand several DNA repair pathways, a welcome development for cancer research.</description>
     <link>http://phys.org/news222516627.html</link>
	 <category>Biology</category>
	 <pubDate>Wed, 20 Apr 2011 11:10:49 EST</pubDate>
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     <title>Researchers get a grip on nervous system's receptors</title>
   	 <description>A digital signal processing technique long used by statisticians to analyze data is helping Houston scientists understand the roots of memory and learning, Alzheimer's and Parkinson's diseases and stroke.</description>
     <link>http://phys.org/news216309912.html</link>
	 <category>Chemistry</category>
	 <pubDate>Mon, 07 Feb 2011 14:40:13 EST</pubDate>
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     <title>Canadian researchers 'see' how to capture CO2</title>
   	 <description>The ability to keep CO2 out of the atmosphere to help prevent climate change is a global issue. The challenge is to use materials that can capture the CO2 and easily release it for permanent storage. Researchers at the University of Calgary and University of Ottawa have provided deeper insights to CO2 capture by &quot;seeing&quot; the exact sites where CO2 is held in a capture material. Their discovery, published in prestigious journal Science, will allow scientists to design better materials to capture more CO2.</description>
     <link>http://phys.org/news207494491.html</link>
	 <category>Chemistry</category>
	 <pubDate>Thu, 28 Oct 2010 14:22:06 EST</pubDate>
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     <title>Crystal clear: Eureka! moment leads to major breakthroughs in structural biology</title>
   	 <description>(PhysOrg.com) -- Tuning out the noise of fellow passengers and the incessant hum of the turbojet engine, Lin Chen pored voraciously over the pages of James Watson's The Double Helix. The words and ideas flowed from the book's pages, drowning out other considerations of how he would spend his life. Eureka! It was his moment of self-realization.</description>
     <link>http://phys.org/news198752862.html</link>
	 <category>Chemistry</category>
	 <pubDate>Mon, 19 Jul 2010 10:20:01 EST</pubDate>
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     <title>Scientists decipher structure of nature's 'light switch'</title>
   	 <description>(PhysOrg.com) -- When the first warm rays of springtime sunshine trigger a burst of new plant growth, it's almost as if someone flicked a switch to turn on the greenery and unleash a floral profusion of color. Opening a window into this process, scientists at the DOE's Brookhaven National Laboratory and collaborators at the University of Wisconsin, Madison, have deciphered the structure of a molecular &quot;switch&quot; much like the one plants use to sense light. Their findings, described online in the Proceedings of the National Academy of Sciences the week of May 31, 2010, help explain how the switch works and could be used to design new ways to modify plant growth.</description>
     <link>http://phys.org/news194505832.html</link>
	 <category>Biology</category>
	 <pubDate>Mon, 31 May 2010 15:00:05 EST</pubDate>
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     <title>Study of alcohol reaction may revolutionize drug development</title>
   	 <description>(PhysOrg.com) -- Enzyme malfunctions are at the root of many serious health problems, but rarely do scientists come up with a way to repair them.</description>
     <link>http://phys.org/news182439565.html</link>
	 <category>Biology</category>
	 <pubDate>Mon, 11 Jan 2010 13:40:41 EST</pubDate>
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     <title>Scientists 'photograph' nano-particle self-assembly</title>
   	 <description>(PhysOrg.com) -- Scientists at the University of Glasgow have imaged the self-assembly of nano-particles, unveiling the blueprint for building designer molecular machines atom-by-atom.</description>
     <link>http://phys.org/news181849583.html</link>
	 <category>Nanotechnology</category>
	 <pubDate>Mon, 04 Jan 2010 17:46:54 EST</pubDate>
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     <title>The hidden lives of proteins</title>
   	 <description>An important Brandeis study appearing in the December 3 issue of Nature raises the curtain on the hidden lives of proteins at the atomic level. The study reports that for the first time, researchers used x-ray crystallography and nuclear magnetic resonance (NMR) techniques to directly visualize protein structures essential for catalysis at the rare high-energy state. The study also showed how the motions of these rare, or hidden, structures collectively, directly contribute to enzyme catalysis.</description>
     <link>http://phys.org/news178987418.html</link>
	 <category>Chemistry</category>
	 <pubDate>Wed, 02 Dec 2009 15:30:01 EST</pubDate>
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